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Chemical chaperones interfere with the formation of scrapie prion protein. | lamine N-oxide (TMAO) and the organic solvent dimethylsulfoxide (DMSO); which we refer to as 'chemical chaperones' because of their influence on protein folding. Although the chemical chaperones did not appear to affect the existing population of PrP(Sc) molecules in ScN2a cells; they did interfere with the formation of PrP(Sc) from newly synthesized PrP(C). We suggest that the chemical chaperones act to stabilize the alpha-helical conformation of PrP(C) and thereby prevent the protein from undergoing a con | 8978663 | [
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Chemical chaperones interfere with the formation of scrapie prion protein. | formational change to produce PrP(Sc). These observations provide further support for the idea that prions arise due to a change in protein conformation and reveal potential strategies for preventing PrP(Sc) formation. | 8978663 | [
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The plastocyanin binding domain of photosystem I. | The molecular recognition between plastocyanin and photosystem I was studied. Photosystem I and plastocyanin can be cross-linked to an active electron transfer complex. Immunoblots and mass spectrometric analysis of proteolytic peptides indicate that the two negative patches conserved in plant plastocyanins are cross-linked with lysine residues of a domain near the N-terminus of the PsaF subunit of photosystem I. Conversion of these negative to uncharged patches of plastocyanin by site-directed mutation D42 | 8978664 | [
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The plastocyanin binding domain of photosystem I. | N/E43Q/D44N/E45Q and E59Q/E60Q/D61N respectively; reveals the first patch to be essential for the electrostatic interaction in the electron transfer complex with photosystem I and the second one to lower the redox potential. The domain in PsaF; not found in cyanobacteria; is predicted to fold into two amphipathic alpha-helices. The interacting N-terminal helix lines up six lysines on one side which may guide a fast one-dimensional diffusion of plastocyanin and provide the electrostatic attraction at the att | 8978664 | [
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The plastocyanin binding domain of photosystem I. | achment site; in addition to the hydrophobic interaction in the area where the electron is transferred to P700 in the reaction center of photosystem I. This two-step interaction is likely to increase the electron transfer rate by more than two orders of magnitude in plants as compared with cyanobacteria. Our data resolve the controversy about the function of PsaF. | 8978664 | [
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Control of neural precursor specification by proneural proteins in the CNS of Drosophila. | Formation of neural precursors in Drosophila is determined by proneural genes. The distinctive pattern of expression of some genes of the achaete-scute complex in the embryonic neuroectoderm has prompted the speculation that they could also function in the specification of neural precursor identity in the CNS. To test this hypothesis; we have analysed the capacity of different proneural proteins to promote the development of a particular CNS precursor; the MP2 precursor. Our results indicate that: (i) all k | 8978666 | [
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Control of neural precursor specification by proneural proteins in the CNS of Drosophila. | nown proneural proteins are similarly able to support the formation of a neural precursor at the position of MP2; (ii) different proneural proteins promote the expression of different characteristics of MP2; and (iii) a totally normal specification of the MP2 fate can only be attained by the proneural genes achaete or scute. | 8978666 | [
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] |
Expression and function of TrkB variants in developing sensory neurons. | Mouse trigeminal neurons survive independently of neurotrophins when their axons are growing to their targets; and are then transiently supported by BDNF before becoming NGF dependent. During the stage of neurotrophin independence; transcripts encoding the BDNF receptor; TrkB; were expressed at very low levels. During the stage of BDNF dependence; high levels of a transcript encoding a receptor with the catalytic tyrosine kinase domain were expressed. Although the levels of this transcript fell as the neuro | 8978665 | [
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Expression and function of TrkB variants in developing sensory neurons. | ns lost responsiveness to BDNF; there were concomitant increases in the expression of transcripts encoding TrkB variants lacking the kinase domain. Analysis of RNA from purified neurons showed that all of these transcripts were present in neurons. BDNF and NGF up-regulated the expression of these transcripts early in development but had little effect later on. To test whether truncated TrkB modulates BDNF signalling via catalytic TrkB; we injected TrkB expression plasmids into NGF-dependent sympathetic neur | 8978665 | [
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Expression and function of TrkB variants in developing sensory neurons. | ons. Whereas expression of catalytic TrkB alone conferred a BDNF survival response; co-expression of non-catalytic TrkB substantially reduced this response. Our results suggest that BDNF responsiveness in sensory neurons during development is modulated by the relative levels of catalytic and non-catalytic TrkB. | 8978665 | [
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TolA central domain interacts with Escherichia coli porins. | TolA is an inner membrane protein with three domains: a transmembrane N-terminus and periplasmic central and C-terminal domains. The interaction of TolA with outer membrane porins of Escherichia coli was investigated. Western blot analyses of cell extracts with anti-TolA antibodies indicated that TolA forms high molecular weight complexes specifically with trimeric OmpF; OmpC; PhoE and LamB; but not with OmpA. The interaction of purified TolA domains with purified porins was also studied. TolA interacted wi | 8978668 | [
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TolA central domain interacts with Escherichia coli porins. | th OmpF; PhoE and LamB porins via its central domain; but not with either their denatured monomeric forms or OmpA. Moreover; the presence or absence of lipopolysaccharides associated with trimeric porins did not modify the interactions. These results suggest that the specific interaction of TolA with outer membrane porins might be relevant to the function of Tol proteins. | 8978668 | [
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Dimerization of TWIK-1 K+ channel subunits via a disulfide bridge. | TWIK-1 is a new type of K+ channel with two P domains and is abundantly expressed in human heart and brain. Here we show that TWIK-1 subunits can self-associate to give dimers containing an interchain disulfide bridge. This assembly involves a 34 amino acid domain that is localized to the extracellular M1P1 linker loop. Cysteine 69 which is part of this interacting domain is implicated in the formation of the disulfide bond. Replacing this cysteine with a serine residue results in the loss of functional K+ | 8978667 | [
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Targeted mutagenesis of acyl-lipid desaturases in Synechocystis: evidence for the important roles of polyunsaturated membrane lipids in growth, respiration and photosynthesis. | Acyl-lipid desaturases introduce double bonds (unsaturated bonds) at specifically defined positions in fatty acids that are esterified to the glycerol backbone of membrane glycerolipids. The desA; desB and desD genes of Synechocystis sp. PCC 6803 encode acyl-lipid desaturases that introduce double bonds at the delta12; omega3 and delta6 positions of C18 fatty acids respectively. The mutation of each of these genes by insertion of an antibiotic resistance gene cartridge completely eliminated the correspondin | 8978669 | [
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Targeted mutagenesis of acyl-lipid desaturases in Synechocystis: evidence for the important roles of polyunsaturated membrane lipids in growth, respiration and photosynthesis. | g desaturation reaction. This system allowed us to manipulate the number of unsaturated bonds in membrane glycerolipids in this organism in a step-wise manner. Comparisons of the variously mutated cells revealed that the replacement of all polyunsaturated fatty acids by a monounsaturated fatty acid suppressed growth of the cells at low temperature and; moreover; it decreased the tolerance of the cells to photoinhibition of photosynthesis at low temperature by suppressing recovery of the photosystem II prote | 8978669 | [
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Targeted mutagenesis of acyl-lipid desaturases in Synechocystis: evidence for the important roles of polyunsaturated membrane lipids in growth, respiration and photosynthesis. | in complex from photoinhibitory damage. However; the replacement of tri- and tetraunsaturated fatty acids by a diunsaturated fatty acid did not have such effects. These findings indicate that polyunsaturated fatty acids are important in protecting the photosynthetic machinery from photoinhibition at low temperatures. | 8978669 | [
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The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin. | The gene encoding the actin-related protein Arp3 was first identified in the fission yeast Schizosaccharomyces pombe and is a member of an evolutionarily conserved family of actin-related proteins. Here we present several key findings that define an essential role for Arp3p in the functioning of the cortical actin cytoskeleton. First; mutants in arp3 interact specifically with profilin and actin mutants. Second; Arp3 localizes to cortical actin patches which are required for polarized cell growth. Third; th | 8978671 | [
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The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin. | e arp3 gene is required for the reorganization of the actin cytoskeleton during the cell cycle. Finally; the Arp3 protein is present in a large protein complex. We believe that this complex may mediate the cortical functions of profilin at actin patches in S. pombe. | 8978671 | [
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Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function. | Profilins bind to monomeric actin and also interact with ligands such as phosphoinositide 4;5-bisphosphate; the proline-rich protein VASP and a complex of four to six polypeptides identified in Acanthamoeba that includes two actin-related proteins. Here; we report the identification and characterization of an essential gene from Schizosaccharomyces pombe; sop2+; a mutation in which rescues the temperature-sensitive lethality of a profilin mutation; cdc3-124. The sop2-1 mutant is defective for cell elongatio | 8978670 | [
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Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function. | n and septation; suggesting that it is involved in multiple cortical actin-requiring processes. Consistent with a role in actin cytoskeletal function; negative interactions have been identified between sop2-1 and act1-48; a mutant allele of actin. Sop2p is a novel 377 amino acid polypeptide with similarity to proteins of the beta-transducin repeat family. Sop2p-related proteins have been identified by sequencing projects in diverse species; and we have isolated a human cDNA highly related to sop2+; SOP2 Hs; | 8978670 | [
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Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function. | which functionally complements the sop2-1 mutation. Sop2p proteins from all species contain peptide sequences identical or highly similar to two peptide sequences from an Acanthamoeba beta-transducin repeat protein present in the profilin binding complex. Biochemical analyses demonstrate that Sop2p is present in a complex which also contains the actin-related protein; Arp3p. Immunofluorescence studies reveal the presence of Sop2p in (i) punctate structures distributed throughout the cell; (ii) cables that | 8978670 | [
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Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function. | extend the length of the cell; and (iii) a medial band in a small percentage of septating cells. Collectively these data demonstrate the interaction of Sop2p with Arp3p; profilin and actin. | 8978670 | [
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Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. | The yeast phosphatidylinositol transfer protein (Sec14p) is required for biogenesis of Golgi-derived transport vesicles and cell viability; and this essential Sec14p requirement is abrogated by inactivation of the CDP-choline pathway for phosphatidylcholine biosynthesis. These findings indicate that Sec14p functions to alleviate a CDP-choline pathway-mediated toxicity to yeast Golgi secretory function. We now report that this toxicity is manifested through the action of yeast Kes1p; a polypeptide that share | 8978672 | [
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Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. | s homology with the ligand-binding domain of human oxysterol binding protein (OSBP). Identification of Kes1p as a negative effector for Golgi function provides the first direct insight into the biological role of any member of the OSBP family; and describes a novel pathway for the regulation of Golgi-derived transport vesicle biogenesis. | 8978672 | [
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Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast. | In eukaryotic cells; monomeric GTPases of the Ypt/Rab family function as regulators at defined steps of vesicular transport in exo- and endocytosis. Here we report on the isolation and characterization of two genes (YPT31 and YPT32) of the yeast Saccharomyces cerevisiae which encode members of the Ypt family exhibiting >80% sequence identity. Whereas the disruption of one of the two genes was phenotypically neutral; the disruption of both YPT31 and YPT32 led to lethality. Depletion of wild-type Ypt31p or of | 8978673 | [
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Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast. | a short-lived ubiquitin-Ypt31p in a ypt32 null background led to a massive accumulation of Golgi-like membranes; an inhibition of invertase secretion and defects in vacuolar protein maturation. Similar alterations were observed in a conditional-lethal ypt31-1 mutant at 30 min after shift to the non-permissive temperature. According to subcellular fractionation; a significant part of Ypt31p appeared to be located in Golgi-enriched membrane fractions. In accordance with this; indirect immunofluorescence usin | 8978673 | [
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Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast. | g affinity-purified anti-Ypt31p antibodies gave a punctate staining similar to that observed with Golgi-located proteins. From the phenotypic alterations observed in ypt31 and ypt32 mutants; it seems likely that the two GTPases are involved in intra-Golgi transport or in the formation of transport vesicles at the most distal Golgi compartment. | 8978673 | [
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Rho guanine nucleotide dissociation inhibitor protein (RhoGDI) inhibits exocytosis in mast cells. | Introducing non-hydrolysable analogues of GTP into the cytosolic compartment of mast cells results in exocytotic secretion through the activation of GTP binding proteins. The identity and mechanism of action of these proteins are not established. We have investigated the effects of Rho GDP dissociation inhibitor (RhoGDI) on exocytosis induced by guanosine 5'-O-(3-thiotriphosphate) (GTP-gamma-S) in rat mast cells; introducing the protein into cells by means of a patch pipette and recording the progress of ex | 8978674 | [
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Rho guanine nucleotide dissociation inhibitor protein (RhoGDI) inhibits exocytosis in mast cells. | ocytosis by monitoring cell capacitance. To allow time for the protein to enter the cells and find its correct location; stimulation was provided 5-10 min after patch rupture by photolysing caged GTP-gamma-S included in the pipette solution. When bovine RhoGDI was introduced into mast cells; exocytosis was inhibited at concentrations of 200-400 nM for native protein and 800 nM to 8 microM for the recombinant form. Protein denatured by heat or N-ethylmaleimide treatment did not inhibit. In permeabilized cell | 8978674 | [
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Rho guanine nucleotide dissociation inhibitor protein (RhoGDI) inhibits exocytosis in mast cells. | s; recombinant RhoGDI increased the rate at which cells lose their ability to respond to GTP-gamma-S. These data demonstrate that one or more small GTP binding proteins of the Rho family has a central role in the exocytotic mechanism in mast cells. | 8978674 | [
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The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. | In the yeast Saccharomyces cerevisiae; the products of at least 15 genes are involved specifically in vesicular transport from the Golgi apparatus to the plasma membrane. Previously; we have shown that three of these genes; SEC6; SEC8 and SEC15; encode components of a multisubunit complex which localizes to the tip of the bud; the predominant site of exocytosis in S. cerevisiae. Mutations in three more of these genes; SEC3; SEC5 and SEC10; were found to disrupt the subunit integrity of the Sec6-Sec8-Sec15 c | 8978675 | [
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The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. | omplex; indicating that these genes may encode some of the remaining components of this complex. To examine this possibility; we cloned and sequenced the SEC5 and SEC10 genes; disrupted them; and either epitope tagged them (Sec5p) or prepared polyclonal antisera (Sec10p) to them for co-immunoprecipitation studies. Concurrently; we biochemically purified the remaining unidentified polypeptides of the Sec6-Sec8-Sec15 complex for peptide microsequencing. The genes encoding these components were identified by c | 8978675 | [
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The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. | omparison of predicted amino acid sequences with those obtained from peptide microsequencing of the purified complex components. In addition to Sec6p; Sec8p and Sec15p; the complex contains the proteins encoded by SEC3; SEC5; SEC10 and a novel gene; EXO70. Since these seven proteins function together in a complex required for exocytosis; and not other intracellular trafficking steps; we have named it the Exocyst. | 8978675 | [
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Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding. | According to the present model for assembly of alphaviruses; e.g. Semliki Forest virus (SFV); the viral genome is first encapsidated into a nucleocapsid (NC) in cytoplasm and this is then used for budding at plasma membrane (PM). The preformed NC is thought to act as a template on which the viral envelope can be organized. In the present work we have characterized two SFV deletion mutants which did not assemble NCs in the cytoplasm but which instead appeared to form NCs at the PM simultaneously with virus b | 8978676 | [
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Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding. | udding. The deletions were introduced in a conserved 14 residue long linker peptide that joins the amino-terminal RNA-binding domain with the carboxy-terminal serine-protease domain of the capsid protein. Despite the deletions and the change in morphogenesis; wild-type (wt)-like particles were produced with almost wt efficiency. It is suggested that the NC assembly defect of the mutants is rescued through spike-capsid interactions at PM. The results show that the preassembly of NCs in the cytoplasm is not a | 8978676 | [
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Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding. | prerequisite for alphavirus budding. The apparent similarities of the morphogenesis pathways of wt and mutant SFV with those of type D and type C retroviruses are discussed. | 8978676 | [
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Uncoupling of stem cell inhibition from monocyte chemoattraction in MIP-1alpha by mutagenesis of the proteoglycan binding site. | We have studied the role of proteoglycans in the function of Macrophage Inflammatory Protein-1 alpha (MIP-1alpha); a member of the proteoglycan binding chemokine family. Sequence and peptide analysis has identified a basic region within MIP-1alpha which appears to be the major determinant of proteoglycan binding and we have now produced a mutant of MIP-1alpha lacking the basic charges on two of the amino acids within this proteoglycan binding site. This mutant (Hep Mut) appears to have lost the ability to b | 8978677 | [
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Uncoupling of stem cell inhibition from monocyte chemoattraction in MIP-1alpha by mutagenesis of the proteoglycan binding site. | ind to proteoglycans. Bioassay of Hep Mut indicates that it has retained stem cell inhibitory properties but has a compromised activity as a monocyte chemoattractant; thus suggesting uncoupling of these two properties of MIP-1alpha. Receptor studies have indicated that the inactivity of Hep Mut on human monocytes correlates with its inability to bind to CCR1; a cloned human MIP-1alpha receptor. In addition; studies using proteoglycan deficient cells transfected with CCR1 have indicated that the proteoglycan | 8978677 | [
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Uncoupling of stem cell inhibition from monocyte chemoattraction in MIP-1alpha by mutagenesis of the proteoglycan binding site. | binding site in MIP-1alpha is a site that is also involved in the docking of MIP-1alpha to the monocyte receptor. The site for interaction with the stem cell receptor must therefore be distinct; suggesting that MIP-1alpha utilizes different receptors for these two different biological processes. | 8978677 | [
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Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton. | Thrombin-stimulated aggregation of human platelets promotes an increase in the phosphatidylinositol 4-phosphate (PtdIns 4-P) 5-kinase (PIPkin) activity in the cytoskeleton. This phenomenon is associated with translocation of PIPkin isoform C to the cytoskeleton and with an increase in the amount of phosphatidylinositol bisphosphate (PtdInsP2) bound to the cytoskeletal pellet. All three of these effects are prevented if the platelets are not stirred or if RGD-containing peptides are present; demonstrating th | 8978678 | [
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] |
Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton. | at they require integrin activation. All three are also abolished by pretreatment with okadaic acid; which also prevents the aggregation-dependent translocation of pp60(c-src) to the cytoskeleton. The results point to the existence of a cytoskeletally associated PtdInsP2 pool under the control of integrin-mediated signals that act via PIPkin C and suggest that a common; okadaic acid-sensitive mechanism may underlie the aggregation-dependent translocation of certain signalling molecules to the platelet cytos | 8978678 | [
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Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton. | keleton. | 8978678 | [
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Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin-dependent pathway. | Constitutive activation of growth factor receptor signaling pathways leads to uncontrolled growth; but why tumor cells become anchorage independent is less clear. The fact that integrins transmit signals required for cell growth suggests that constitutive activation of steps downstream from integrins mediates anchorage independence. Since the small GTPase Rho may mediate integrin signal transduction; the effects of serum and the Rho nucleotide exchange factor oncogenes dbl and lbc on cell growth and signali | 8978679 | [
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Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin-dependent pathway. | ng pathways were examined. Our data show that these oncogenes induce anchorage-independent but serum-dependent growth and stimulation of signaling pathways. These results show; therefore; that anchorage-independent growth results from constitutive activation of integrin-dependent signaling events. They also support the view that Rho is a functionally important mediator of integrin signaling. | 8978679 | [
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Mechanism of activation of protein kinase B by insulin and IGF-1. | Insulin activated endogenous protein kinase B alpha (also known as RAC/Akt kinase) activity 12-fold in L6 myotubes; while after transfection into 293 cells PKBalpha was activated 20- and 50-fold in response to insulin and IGF-1 respectively. In both cells; the activation of PKBalpha was accompanied by its phosphorylation at Thr308 and Ser473 and; like activation; phosphorylation of both of these residues was prevented by the phosphatidylinositol 3-kinase inhibitor wortmannin. Thr308 and/or Ser473 were mutat | 8978681 | [
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Mechanism of activation of protein kinase B by insulin and IGF-1. | ed to Ala or Asp and activities of mutant PKBalpha molecules were analysed after transfection into 293 cells. The activity of wild-type and mutant PKBalpha was also measured in vitro after stoichiometric phosphorylation of Ser473 by MAPKAP kinase-2. These experiments demonstrated that activation of PKBalpha by insulin or insulin-like growth factor-1 (IGF-1) results from phosphorylation of both Thr308 and Ser473; that phosphorylation of both residues is critical to generate a high level of PKBalpha activity | 8978681 | [
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Mechanism of activation of protein kinase B by insulin and IGF-1. | and that the phosphorylation of Thr308 in vivo is not dependent on phosphorylation of Ser473 or vice versa. We propose a model whereby PKBalpha becomes phosphorylated and activated in insulin/IGF-1-stimulated cells by an upstream kinase(s). | 8978681 | [
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Tyrosine-599 of the c-Mpl receptor is required for Shc phosphorylation and the induction of cellular differentiation. | Interaction of thrombopoietin (TPO) with its receptor; c-Mpl; triggers cell growth and differentiation responses controlling primitive haemopoietic cell production and megakaryocytopoiesis. To examine the important receptor domains and signal transduction pathways involved in these cellular responses; c-Mpl cytoplasmic domain truncation and tyrosine substitution mutants were generated. In the myelomonocytic leukaemia cell lines WEHI3B-D+ and M1; ectopic expression of the wild-type c-Mpl receptor induced TPO | 8978680 | [
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Tyrosine-599 of the c-Mpl receptor is required for Shc phosphorylation and the induction of cellular differentiation. | -dependent cellular differentiation characterized by increased cell migration through agar and acquisition of the morphology and molecular markers of macrophages. Consistent with the concept that proliferative and differentiation signals emanate from distinct receptor domains; the C-terminal 33 amino acids of c-Mpl were dispensable for a proliferative response in Ba/F3 cells but proved critical for WEHI3B-D+ and M1 differentiation. Finer mapping revealed that substitution of Tyr599 by phenylalanine within t | 8978680 | [
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Tyrosine-599 of the c-Mpl receptor is required for Shc phosphorylation and the induction of cellular differentiation. | his c-Mpl domain was sufficient to abolish the normal differentiation response. Moreover; in contrast to the normal c-Mpl receptor; this same mplY599F mutant was also incapable of stimulating TPO-dependent Shc phosphorylation; the association of Shc with Grb2 or c-Mpl and of inducing c-fos expression. Thus activation of components of the Ras signalling cascade; initiated by interaction of Shc with c-Mpl Tyr599; may play a decisive role in specific differentiation signals emanating from the c-Mpl receptor. | 8978680 | [
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The p38 and ERK MAP kinase pathways cooperate to activate Ternary Complex Factors and c-fos transcription in response to UV light. | We investigated the activation of c-fos transcription following UV irradiation; a 'stress' stimulus. In both HeLa TK- and NIH 3T3 cells the Serum Response Element is required for efficient UV-induced c-fos transcription; and in HeLa TK- cells the Ternary Complex Factor (TCF) binding site contributes substantially to activation. Consistent with this; UV irradiation activates LexA-TCF fusion proteins more strongly in HeLa TK- than in NIH 3T3 cells. The TCF C-termini of the TCFs are substrates for UV-induced M | 8978682 | [
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The p38 and ERK MAP kinase pathways cooperate to activate Ternary Complex Factors and c-fos transcription in response to UV light. | AP kinases: both the Elk-1 and SAP-1a C-termini are efficiently phosphorylated by the p38 MAPK; but only the Elk-1 C-terminus is a good substrate for the SAPK/JNKs. The specificity and activation kinetics of TCF C-terminal kinases; and the susceptibility of transcriptional activation by LexA-TCF fusion proteins to specific inhibitors of different MAPK pathways; show that both the ERK and p38 MAPK pathways contribute to TCF activation in response to UV irradiation. Activity of both these pathways is also req | 8978682 | [
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The p38 and ERK MAP kinase pathways cooperate to activate Ternary Complex Factors and c-fos transcription in response to UV light. | uired for the response of the c-fos gene itself to UV stimulation. | 8978682 | [
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A novel chloride channel in Vicia faba guard cell vacuoles activated by the serine/threonine kinase, CDPK. | Calcium-Dependent Protein Kinases (CDPKs) in higher plants contain a C-terminal calmodulin-like regulatory domain. Little is known regarding physiological CDPK targets. Both kinase activity and multiple Ca2+-dependent signaling pathways have been implicated in the control of stomatal guard cell movements. To determine whether CDPK or other protein kinases could have a role in guard cell signaling; purified and recombinant kinases were applied to Vicia faba guard cell vacuoles during patch-clamp experiments. | 8978683 | [
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] |
A novel chloride channel in Vicia faba guard cell vacuoles activated by the serine/threonine kinase, CDPK. | CDPK activated novel vacuolar chloride (VCL) and malate conductances in guard cells. Activation was dependent on both Ca2+ and ATP. Furthermore; VCL activation occurred in the absence of Ca2+ using a Ca2+-independent; constitutively active; CDPK* mutant. Protein kinase A showed weaker activation (22% as compared with CDPK). Current reversals in whole vacuole recordings shifted with the Nernst potential for Cl-and vanished in glutamate. Single channel recordings showed a CDPK-activated 34 +/- 5 pS Cl- chann | 8978683 | [
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A novel chloride channel in Vicia faba guard cell vacuoles activated by the serine/threonine kinase, CDPK. | el. VCL channels were activated at physiological potentials enabling Cl- uptake into vacuoles. VCL channels may provide a previously unidentified; but necessary; pathway for anion uptake into vacuoles required for stomatal opening. CDPK-activated VCL currents were also observed in red beet vacuoles suggesting that these channels may provide a more general mechanism for kinase-dependent anion uptake. | 8978683 | [
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The Drosophila phosphoinositide 3-kinase Dp110 promotes cell growth. | Phosphoinositide 3-kinases (PI3Ks) have been identified in an evolutionarily diverse range of organisms; including mammals; Drosophila; yeast; plants and Dictyostelium. They are activated by a multitude of extracellular signals and implicated in mitogenesis; differentiation and cell survival; as well as in the control of the cytoskeleton and cell shape. Here we describe the molecular and functional analysis of Drosophila p110 (Dp110). A full-length Dp110 cDNA was isolated and found to encode a protein homol | 8978685 | [
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The Drosophila phosphoinositide 3-kinase Dp110 promotes cell growth. | ogous throughout its length to the class I mammalian PI3Ks p110alpha and p110beta. Overexpression of Dp110 in wing or eye imaginal discs resulted in flies with enlarged wings or eyes respectively. In contrast; overexpression of Dp110 containing a mutation predicted to result in the loss of catalytic activity resulted in smaller wings and eyes. The alterations in wing size result from changes in both cell size and cell number; whereas in the eye only differences in cell size were detected. These data imply a | 8978685 | [
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The Drosophila phosphoinositide 3-kinase Dp110 promotes cell growth. | role for Dp110 in growth control during Drosophila development and have implications for the function of class I PI3Ks in other organisms. | 8978685 | [
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Yeast Gpi8p is essential for GPI anchor attachment onto proteins. | Glycosylphosphatidylinositol (GPI) anchors are added onto newly synthesized proteins in the ER. Thereby a putative transamidase removes a C-terminal peptide and attaches the truncated protein to the free amino group of the preformed GPI. The yeast mutant gpi8-1 is deficient in this addition of GPIs to proteins. GPI8 encodes for an essential 47 kDa type I membrane glycoprotein residing on the luminal side of the ER membrane. GPI8 shows significant homology to a novel family of vacuolar plant endopeptidases o | 8978684 | [
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Yeast Gpi8p is essential for GPI anchor attachment onto proteins. | ne of which is supposed to catalyse a transamidation step in the maturation of concanavalin A and acts as a transamidase in vitro. Humans have a gene which is highly homologous to GPI8 and can functionally replace it. | 8978684 | [
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Growth arrest by the cyclin-dependent kinase inhibitor p27Kip1 is abrogated by c-Myc. | We show here that c-Myc antagonizes the cyclin-dependent kinase (CDK) inhibitor p27Kip1. p27 expressed from recombinant retroviruses in Rat1 cells associated with and inhibited cyclin E/CDK2 complexes; induced accumulation of the pRb and p130 proteins in their hypophosphorylated forms; and arrested cells in G1. Prior expression of c-Myc prevented inactivation of cyclin E/CDK2 as well as dephosphorylation of pRb and p130; and allowed continuous cell proliferation in the presence of p27. This effect did not r | 8978686 | [
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Growth arrest by the cyclin-dependent kinase inhibitor p27Kip1 is abrogated by c-Myc. | equire ubiquitin-mediated degradation of p27. Myc altered neither the susceptibility of cyclin E/CDK2 to inhibition by p27; nor the intrinsic CDK-inhibitory activity of p27; but induced sequestration of p27 in a form unable to bind cyclin E/CDK2. Neither Myc itself nor other G1-cyclin/CDK complexes were directly responsible for p27 sequestration. Retroviral expression of G1 cyclins (D1-3; E or A) or of the Cdc25A phosphatase did not overcome p27-induced arrest. Growth rescue by Myc required dimerization wit | 8978686 | [
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Growth arrest by the cyclin-dependent kinase inhibitor p27Kip1 is abrogated by c-Myc. | h Max; DNA binding and an intact transcriptional activation domain; as previously shown for cellular transformation. We propose that this activity is mediated by the product of an as yet unknown Myc-Max target gene(s) and represents an essential aspect of Myc's mitogenic and oncogenic functions. | 8978686 | [
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Fission yeast Cut1 and Cut2 are essential for sister chromatid separation, concentrate along the metaphase spindle and form large complexes. | Fission yeast Schizosaccharomyces pombe temperature-sensitive (ts) cut1 mutants fail to separate sister chromatids in anaphase but the cells continue to divide; leading to bisection of the undivided nucleus (the cut phenotype). If cytokinesis is blocked; replication continues; forming a giant nucleus with polyploid chromosomes. We show here that the phenotype of ts cut2-364 is highly similar to that of cut1 and that the functions of the gene products of cut1+ and cut2+ are closely interrelated. The cut1+ an | 8978688 | [
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Fission yeast Cut1 and Cut2 are essential for sister chromatid separation, concentrate along the metaphase spindle and form large complexes. | d cut2+ genes are essential for viability and interact genetically. Cut1 protein concentrates along the short spindle in metaphase as does Cut2. Cut1 (approximately 200 kDa) and Cut2 (42 kDa) associate; as shown by immunoprecipitation; and co-sediment as large complexes (30 and 40S) in sucrose gradient centrifugation. Their behavior in the cell cycle is strikingly different; however: Cut2 is degraded in anaphase by the same proteolytic machinery used for the destruction of cyclin B; whereas Cut1 exists thro | 8978688 | [
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Fission yeast Cut1 and Cut2 are essential for sister chromatid separation, concentrate along the metaphase spindle and form large complexes. | ughout the cell cycle. The essential function of the Cut1-Cut2 complex which ensures sister chromatid separation may be regulated by Cut2 proteolysis. The C-terminal region of Cut1 is evolutionarily conserved and similar to that of budding yeast Esp1; filamentous fungi BimB and a human protein. | 8978688 | [
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The fission yeast dma1 gene is a component of the spindle assembly checkpoint, required to prevent septum formation and premature exit from mitosis if spindle function is compromised. | Premature initiation of cytokinesis can lead to loss of chromosomes; and 'cutting' of the nucleus. Therefore; the proper spatial and temporal co-ordination of mitosis and cytokinesis is essential for maintaining the integrity of the genome. The fission yeast cdc16 gene is implicated both in the spindle assembly checkpoint and control of septum formation. To identify other proteins involved in these controls; we have isolated multicopy suppressors of the cdc16-116 mutation; and the characterization of one of | 8978687 | [
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The fission yeast dma1 gene is a component of the spindle assembly checkpoint, required to prevent septum formation and premature exit from mitosis if spindle function is compromised. | these; dma1 (defective in mitotic arrest); is presented here. dma1 is not an essential gene; but in a dma1 null background (dma1-D1) the function of the spindle assembly checkpoint is compromised. If assembly of the spindle is prevented; dma1-D1 cells do not arrest; the activity of cdc2 kinase decays and cells form a division septum without completing a normal mitosis. dma1-D1 cells also show an increased rate of chromosome loss during exponential growth. Upon ectopic expression from an inducible promoter; | 8978687 | [
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Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphase is lessened by the dosage increase of a novel gene sds23+. | Ubiquitin-dependent proteolysis is required for the onset of anaphase. We show that protein dephosphorylation by protein phosphatase 1 (PP1) is also essential for initiating anaphase in fission yeast. PP1 may directly or indirectly regulate the 20S cyclosome/APC (anaphase-promoting complex) required for anaphase-promoting proteolysis. Using anti-phosphopeptide antibodies; PP1 is shown to be dephosphorylated at the C-terminus; upon the onset of anaphase; for reactivation. sds23+; a novel gene; is a multicopy | 8978689 | [
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Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphase is lessened by the dosage increase of a novel gene sds23+. | suppressor for mutations in PP1 and the 20S cyclosome/APC; implying that the gene dosage increase can relieve the requirement for PP1 and the cyclosome/APC for the onset of anaphase. The sds23+ gene is not essential for cell viability; but a mutant with the gene deleted cannot form colonies at 22 and 36 degrees C. In the sds23 deletion mutant; the progression of anaphase and cytokinesis is retarded and cell shape is aberrant. These defects are overcome by plasmids carrying the genes encoding subunits of th | 8978689 | [
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Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphase is lessened by the dosage increase of a novel gene sds23+. | e 20S cyclosome/APC or PP1. These results demonstrate functions other than promoting anaphase for the components of the 20S cyclosome/APC and also a close functional relationship of Sds23 with PP1 and 20S cyclosome/APC. | 8978689 | [
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The Schizosaccharomyces pombe rad3 checkpoint gene. | The rad3 gene of Schizosaccharomyces pombe is required for checkpoint pathways that respond to DNA damage and replication blocks. We report the complete rad3 gene sequence and show that rad3 is the homologue of Saccharomyces cerevisiae ESR1 (MEC1/SAD3) and Drosophila melanogaster mei-41 checkpoint genes. This establishes Rad3/Mec1 as the only conserved protein which is required for all the DNA structure checkpoints in both yeast model systems. Rad3 is an inessential member of the 'lipid kinase' subclass of | 8978690 | [
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The Schizosaccharomyces pombe rad3 checkpoint gene. | kinases which includes the ATM protein defective in ataxia telangiectasia patients. Mutational analysis indicates that the kinase domain is required for Rad3 function; and immunoprecipitation of overexpressed Rad3 demonstrates an associated protein kinase activity. The previous observation that rad3 mutations can be rescued by a truncated clone lacking the kinase domain may be due to intragenic complementation. Consistent with this; biochemical data suggest that Rad3 exists in a complex containing multiple | 8978690 | [
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The Schizosaccharomyces pombe rad3 checkpoint gene. | copies of Rad3. We have identified a novel human gene (ATR) whose product is closely related to Rad3/Esr1p/Mei-41. ATR can functionally complement esr1-1 radiation sensitivity in S. cerevisiae. Together; the structural conservation and functional complementation suggest strongly that the mechanisms underlying the DNA structure checkpoints are conserved throughout evolution. | 8978690 | [
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Targeting presequence acquisition after mitochondrial gene transfer to the nucleus occurs by duplication of existing targeting signals. | We have cloned a gene for mitochondrial ribosomal protein S11 (RPS11); which is encoded in lower plants by the mitochondrial genome; in higher plants by the nuclear genome; demonstrating genetic information transfer from the mitochondrial genome to the nucleus during flowering plant evolution. The sequence s11-1 encodes an N-terminal extension as well as an organelle-derived RPS11 region. Surprisingly; the N-terminal region has high amino acid sequence similarity with the presequence of the beta-subunit of | 8978691 | [
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Targeting presequence acquisition after mitochondrial gene transfer to the nucleus occurs by duplication of existing targeting signals. | ATP synthase from plant mitochondria; suggesting a common lineage of the presequences. The deduced N-terminal region of s11-2; a second nuclear-encoded homolog of rps11; shows high sequence similarity with the putative presequence of cytochrome oxidase subunit Vb. The sharing of the N-terminal region together with its 5' flanking untranslated nucleotide sequence in different proteins strongly suggests an involvement of duplication/recombination for targeting signal acquisition after gene migration. A remnan | 8978691 | [
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Targeting presequence acquisition after mitochondrial gene transfer to the nucleus occurs by duplication of existing targeting signals. | t of ancestral rps11 sequence; transcribed and subjected to RNA editing; is found in the mitochondrial genome; indicating that inactivation of mitochondrial rps11 gene expression was initiated at the translational level prior to termination of transcription. | 8978691 | [
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Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. | Repair of a uracil-guanine base pair in DNA has been reconstituted with the recombinant human proteins uracil-DNA glycosylase; apurinic/apyrimidinic endonuclease; DNA polymerase beta and DNA ligase III. The XRCC1 protein; which is known to bind DNA ligase III; is not absolutely required for the reaction but suppresses strand displacement by DNA polymerase beta; allowing for more efficient ligation after filling of a single nucleotide patch. We show that XRCC1 interacts directly with DNA polymerase beta usin | 8978692 | [
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Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. | g far Western blotting; affinity precipitation and yeast two-hybrid analyses. In addition; a complex formed between DNA polymerase beta and a double-stranded oligonucleotide containing an incised abasic site was supershifted by XRCC1 in a gel retardation assay. The region of interaction with DNA polymerase beta is located within residues 84-183 in the N-terminal half of the XRCC1 protein; whereas the C-terminal region of XRCC1 is involved in binding DNA ligase III. These data indicate that XRCC1; which has | 8978692 | [
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Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. | no known catalytic activity; might serve as a scaffold protein during base excision-repair. DNA strand displacement and excessive gap filling during DNA repair were observed in cell-free extracts of an XRCC1-deficient mutant cell line; in agreement with the results from the reconstituted system. | 8978692 | [
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ORC- and Cdc6-dependent complexes at active and inactive chromosomal replication origins in Saccharomyces cerevisiae. | We have developed a genomic footprinting protocol which allows us to examine protein-DNA interactions at single copy chromosomal origins of DNA replication in the budding yeast Saccharomyces cerevisiae. We show that active replication origins oscillate between two chromatin states during the cell cycle: an origin recognition complex (ORC)-dependent post-replicative state and a Cdc6p-dependent pre-replicative state. Furthermore; we show that both post- and pre-replicative complexes can form efficiently on cl | 8978693 | [
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ORC- and Cdc6-dependent complexes at active and inactive chromosomal replication origins in Saccharomyces cerevisiae. | osely apposed replicators. Surprisingly; ARS301 which is active as an origin on plasmids but not in its normal chromosomal location; forms ORC- and Cdc6p-dependent complexes in both its active and inactive contexts. Thus; although ORC and Cdc6p are essential for initiation; their binding is not sufficient to dictate origin use. | 8978693 | [
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] |
The helix-loop-helix transcription factor SEF-2 regulates the activity of a novel initiator element in the promoter of the human somatostatin receptor II gene. | The effects of somatostatin hormones are mediated by a family of five different seven-helix transmembrane spanning receptors (SSTR1-5). The expression of the five different SSTR subtypes displays a complex temporal- and tissue-specific pattern. To investigate the molecular mechanisms controlling the different expression patterns of the SSTRs; we cloned the 5'-flanking region of the human SSTR2 gene. Characterization of the SSTR2 promoter resulted in the identification of a novel initiator element (SSTR2inr) | 8978694 | [
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] |
The helix-loop-helix transcription factor SEF-2 regulates the activity of a novel initiator element in the promoter of the human somatostatin receptor II gene. | . Transcriptional activity of the SSTR2inr is dependent on the presence of a binding site (E-box) for basic helix-loop-helix (bHLH) transcription factors. By screening a mouse brain cDNA expression library we isolated a cDNA coding for the bHLH transcription factor SEF-2. SEF-2 binds to the E-box present in the SSTR2inr; both in vitro and in vivo and activates transcription from the SSTR2inr. A single point mutation within the E-box eliminates binding of SEF-2 and results in a complete loss of transcription | 8978694 | [
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] |
The helix-loop-helix transcription factor SEF-2 regulates the activity of a novel initiator element in the promoter of the human somatostatin receptor II gene. | al activity of the SSTR2inr. Furthermore; DNA binding studies demonstrate that the basal transcription factor TFIIB can be tethered to the SSTR2inr through physical interaction with SEF-2. In summary; the SSTR2inr represents a novel type of initiator element that confers gene expression in the absence of a TATA-box or binding sites for other known initiator factors; like YY-1 or USF. | 8978694 | [
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A T cell controlled molecular pathway regulating the IgH locus: CD40-mediated activation of the IgH 3' enhancer. | Immunoglobulin heavy chain (IgH) class switch recombination and regulation of IgH expression levels are processes suggested to be controlled by the IgH 3' enhancer. Here we demonstrate that CD40 or IgM receptor stimulation of primary B cells results in transactivation of this enhancer. 4-Hydroxy-3-nitrophenylacetyl (NIP)-BSA induction of a K46 B cell line expressing a chimeric NIP-specific CD40 single chain receptor results in a ligand receptor-dependent response of a 3' enhancer ETS/AP-1 minimal promoter c | 8978695 | [
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A T cell controlled molecular pathway regulating the IgH locus: CD40-mediated activation of the IgH 3' enhancer. | onstruct. Gel retardation analysis and genomic footprinting experiments reveal that CD40 or IgM induction recruits NFAB (nuclear factors of activated B cells) to the ETS/AP-1 motif. While IgM signalling recruits c-Fos; JunB and Elf-1 (NFAB-I); only JunB and Elf-1 were observed following CD40 signalling (NFAB-II). CD40 signalling; however; induces a Fos family-related partner for JunB; which may account for the transcriptional activity observed by NFAB-II in K46 cells. We propose a model whereby CD40 and IgM | 8978695 | [
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A T cell controlled molecular pathway regulating the IgH locus: CD40-mediated activation of the IgH 3' enhancer. | receptor-mediated signalling converge in the process of 3' enhancer activation in B lymphocytes. Our data provide a putative molecular explanation as to why CD40L-deficient mice; and possibly patients with hyper-IgM syndrome; are unable to undergo T cell-dependent class switch recombination but respond properly upon lipopolysaccharide-induced switch recombination. | 8978695 | [
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A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. | Nuclear receptors (NRs) are ligand-inducible transcription factors that mediate complex effects on development; differentiation and homeostasis. They regulate the transcription of their target genes through binding to cognate DNA sequences as homodimers or heterodimers. The molecular mechanisms underlying transcriptional activation by NRs are still poorly understood; although intermediary factors (mediators) appear to be involved in mediating the transactivation functions of NRs. TIF1 has been identified pr | 8978696 | [
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A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. | eviously as a protein that interacts specifically with the ligand binding domain of several nuclear receptors; both in yeast and in vitro. The characteristics of these interactions have led us to suggest that TIF1 might be a mediator of the NR ligand-inducible activation function AF-2. Using a two-hybrid screening in yeast; we have now identified two TIF1-binding proteins; mHP1 alpha and mMOD1; that are mouse homologues of the Drosophila heterochromatinic protein 1. Using mHP1 alpha as a bait in a second tw | 8978696 | [
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A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. | o-hybrid screening; we have isolated cDNAs encoding proteins that are also very likely to be involved in chromatin structure and function; as well as a protein structurally and functionally related to TIF1 (renamed TIF1 alpha); which was named TIF1 beta. Here we discuss how the function of members of the TIF1 family in the control of transcription could be exerted at the level of the structure of the chromatin template. | 8978696 | [
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Different mechanisms control signal-induced degradation and basal turnover of the NF-kappaB inhibitor IkappaB alpha in vivo. | The transcription factor NF-kappaB is sequestered in the cytoplasm by a family of IkappaB molecules. Upon cellular stimulation with diverse agents; one of these molecules; IkappaB alpha; is rapidly phosphorylated and subsequently degraded. This process triggers nuclear translocation of NF-kappaB and the successive activation of target genes. Independent of its rapid stimulation-induced breakdown; IkappaB alpha is inherently unstable and undergoes a continuous turnover. To compare the mechanisms and protein | 8978697 | [
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Different mechanisms control signal-induced degradation and basal turnover of the NF-kappaB inhibitor IkappaB alpha in vivo. | domains involved in inducible and basal degradation of IkappaB alpha in intact cells we employed a transfection strategy using tagged IkappaB alpha and ubiquitin molecules. We show that tumor necrosis factor alpha (TNFalpha) induced breakdown of IkappaB alpha but not its basal turnover coincides with ubiquitination in the amino-terminal signal response domain (SRD) of IkappaB alpha. Neither the SRD nor the carboxy-terminal PEST sequence is needed for basal turnover; which instead depends only on the core an | 8978697 | [
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Different mechanisms control signal-induced degradation and basal turnover of the NF-kappaB inhibitor IkappaB alpha in vivo. | kyrin repeat domain. Despite the differences in the requirements of protein domains and ubiquitin-conjugation for both degradation pathways; each one is mediated by the proteasome. This finding is important for understanding alternative modes of controlling NF-kappaB activity. | 8978697 | [
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Function of the Evx-2 gene in the morphogenesis of vertebrate limbs. | Vertebrate gene members of the HoxD complex are essential for proper development of the appendicular skeletons. Inactivation of these genes induces severe alterations in the size and number of bony elements. Evx-2; a gene related to the Drosophila even-skipped (eve) gene; is located close to Hoxd-13 and is expressed in limbs like the neighbouring Hoxd genes. To investigate whether this tight linkage reflects a functional similarity; we produced a null allele of Evx-2. Furthermore; and because Hoxd-13 functi | 8978698 | [
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Function of the Evx-2 gene in the morphogenesis of vertebrate limbs. | on is prevalent over that of nearby Hoxd genes; we generated two different double mutant loci wherein both Evx-2 and Hoxd-13 were inactivated in cis. The analysis of these various genetic configurations revealed the important function of Evx-2 during the development of the autopod as well as its genetic interaction with Hoxd-13. These results show that; in limbs; Evx-2 functions like a Hoxd gene. A potential evolutionary scenario is discussed; in which Evx-2 was recruited by the HoxD complex in conjunction | 8978698 | [
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Function of the Evx-2 gene in the morphogenesis of vertebrate limbs. | with the emergence of digits in an ancestral tetrapod. | 8978698 | [
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