EMBO/sd-character-level-ner huggingface dataset:
Representative bright field microscopic images of TDP-43 condensates (in Hepes buffer), Bar, 25 µm (F) and quantification of condensate number (G) Box plots show the comparison of median and inter-quartile range (upper and lower quartiles) of all fields of view (FOV) from Min to Max (whiskers) of two replicates (≥ 22 FOV per condition). *p < 0.0332, **p < 0.0021 and ***p < 0.0002 by one-way ANOVA with Dunnett´s multiple comparison test to Wt, comparing the respective concentration condition (5, 10, 20 µM).
(a) Schematic of experimental workflow. DLD1 cells were converted to SILAC medium, incubated overnight in the presence or absence of 5 μM PIK-III, lysed, and ubiquitin-modified peptides enriched with anti-diglycyl antibody and quantified as described in the Methods.
C. Confirmation of Lamin B1 overexpression by immunocytochemistry in NPCs. Scale bar = 10 µm.
D Read coverage of SRSF2 from the indicated RNA-seq sample data with or without UPF3A siRNA treatment shown as Integrative Genomics Viewer (IGV) snapshot. The canonical and NMD-sensitive isoforms are schematically indicated below. Quantification of gene expression and isoform usage by IsoformSwitchAnalyzeR (right).
(A, B) U2OS Flp-In/T-REx cells with integrated transgenes encoding GFP-BRCA1BRCT or -BRCA1BRCT S1655A were transfected with non-targeting siRNA (CTRL) or siRNA targeting RAP80 or BRCA1. Following doxycycline treatment to induce transgene expression (5 μg/mL, 24 h), cells were irradiated (10 Gy) and processed for immunofluorescence 1 h post-IR for GFP and antibodies against RAP80 and γH2AX. Shown in (A) is the quantitation of a minimum of 100 cells per replicate where the bars represent the mean ± S.D (n=4). Representative micrographs are shown in (B).
(A,B) Cumulative risk for ICU admission (A) and cumulative survival (B) in COV patients (n=111), grouped for cut-off value of S1P serum level of 0.60 μM. Statistical analysis was performed by Cox regression. Exact p values are reported.
G. Quantification of the MAM:mitochondrion ratio of TOM20 immunogold particles from E under normoxic and hypoxic (1% O2) conditions. Data (mean ± s.e.m.) are from 3 independent experiments. n = 50 MAMs (one MAM means one mitochondrial ER tethering site in the corresponding mitochondria). NS means not significant.
C Experimental workflow: equimolar amounts of 5' and 3' gRNA-containing RNPs (fluorescently tagged with ATTO-550) were nucleofected into resting CD4 T cells, which were stimulated after 48 hours with anti-CD2/3/28 microbeads and IL-2.
C. Control and OMA1 KO HCT116 cells were treated with DMSO or 1mM DMOG in fresh medium for 12 h. Subsequent injections of glucose, oligomycin (Oligo), and 2-deoxy-glucose (2-DG) were performed as indicated. The extracellular acidification rates (ECAR) were measured with a Seahorse Extracellular Flux Analyzer XF96. The data are presented as mean ± SD (n = 3 independent experiments).
(A) Experimental set-up used to assay transfer through conditioned medium (upper scheme) and cell-to-cell contacts (lower scheme) in neurons. For the CM experiments, donor neurons are loaded with α-synucleinfibrils for 16 hours, washed 3 times with PBS and then fresh medium is added and left to condition for 72 hours. CM is then collected and transferred to acceptor neurons (10 div) for 72 hours. In the cell-to-cell contact impairment (No contact) experiment the donor (already loaded) and newly dissected acceptor (already labelled) neurons are plated on different coverslips placed in the same Petri dish. In both experiments, the percentage of cells containing α-synucleinATTO-550puncta, and the number and mean size of α-synucleinpuncta per cell are quantified using the ICY software after 72 hours.
F) Kinetics of the expression of tBID-GFP (blue) and PI intake upon tBID expression (purple) and unstransfected HCT116 AKO cells (in grey). Plots show the average fluorescence intensity (dark lines) and its standard deviation (shaded areas) from 3 technical replicates and 3 independent experiments. Fluorescence intensity was obtained by analysis the total fluorescence per well using incucyte system every 60 min.
Indirect immunofluorescence analysis of mAtg9 with (D)HA-full‐length p38IP (HA-FL), (E)HA-C‐terminal p38IP (HA-CT), and (F) HA-N‐terminal p38IP (HA-NT). Bars=5 μm. The co‐localization seen in (D) and (E) was not because of overlap of randomly distributed vesicles. Cross‐correlation function (CCF) analysis ( van Steensel et al, 1996) showed a peak and maximum Rp value around ΔX=0, indicating that co‐localization between mAtg9 and p38IP is positively correlated and non random ( Supplementary Figure S1).
A. STING protein expression of 58 colon adenocarcinoma specimens within the TCGA COAD collection were obtained from the CPTAC project website. Samples were partitioned into STING-Low (non-detectable STING protein, N=15) and STING-Hi (detectable STING protein, N=43) groups. Kaplan Meier curve is shown with P value indicated.
(B) Western blot analysis shows that the level of PI4K2A expression was closely matched with that of wild-type cells.
(E) Axonal spheroids in npc1−/− mice. Spheroids (arrows), seen as Calbindin-positive (red) swellings surrounded by myelin (anti-myelin basic protein; green), are numerous in the npc1−/− cerebellum (50-d-old, lobule X shown) but are not seen in the wild-type control. Bar = 5 μm.
Model of TRSE (red) and Omp25 (green) labeling corresponding to (A). Incorporation of new material at the pole and/or at the constriction site is shown as black areas.
(H) ROC curve derived from Bayesian regularized neural networks (BRNN) based on four GM3 species in (G).
(D, E) Immunohistochemistry (D) and quantitative analysis (E) of dystrophin-positive fibers in mdx TA muscles treated with single intramuscular injection of 0.5 μg PMO mixed with MOTS-c (20 μg) (PMO-M) or PMO alone (scale bar: 100 μm) (n=3; **p<0.001). C57 means wild-type control C57BL/6.
Decreased PSD density, but not PSD length, thickness, or perforation (%), in the Ptprd-/- SLM (P21; male), revealed by EM. Arrows in panel K indicate PSDs.
(E) Pexophagy as assayed by Pex11-GFP western blot of cells grown for up to 3 days in glucose, oleate or glycerol medium. Samples of WT cells (left panel) and atg36Δ cells (right panel) were taken from the cultures after 24, 48 and 72 h.
Immunoprecipitations of HA-tagged KRAB domains in order to check  interaction with cKAP1. Co-transfection of Flag-tagged cKAP1 (upper panel) or Flag-tagged hKAP1 (lower panel) and HA-tagged ZNF398 DUF3669 domain negative control, H2ZYM4 and M3XKG1 cKRAB domains and ZNF93 hKRAB domain in KAP1 KO HAP1 cells followed by HA-immunoprecipitation. cKAP1 and hKAP1 presence was revealed by Western-Blot using an anti-Flag antibody. Input = Cellular lysate, IP = Immunoprecipitate. Western-Blot using an HA antibody on the IPs at the bottom.
Representative images showing the morphologic changes of hOSE-MXIV, hOSE-YAP and hOSE-YAPS127A cells at passage 7. Scale bar: 50 µm.
Enriched gene ontology classes of uninfected (C) and PAO1-infected (D) lungs. Red bar, GO class of up-regulated gene in LL-37+/+ mice. Blue bar, GO class of up-regulated gene in wild type FVB mouse lung. GO terms were ranked by the enrichment P-value. E. Protein-protein interaction network of selected genes with high expression level in PAO1-infected wild-type lung (blue) and PAO1-infected LL-37+/+ lung (red), respectively.
(a) Rubicon siRNA treatment of the NIH 3T3 cells led to decreased levels of p62 and LC3 II under both normal and nutrient-starvation conditions.
B. Log-odd ratio of random sampling from mass spectrometry background. In blue is the distribution upon random sampling (x1000) from tissue proteins. Red dot indicated the true values of analysis. In APR regions the actual value (red) resides either in the edges or outside of the random distribution. (statistics: Z-test). * P ≤0.05, ** P≤0.01, *** P≤0.001, **** P≤0.0001
(I-L) Control and IRGM knockdown THP-1 IFN reporter cells were treated with (I) Poly I:C (1 μg/ml) for 8 h, 12 h and 24 h or (J) Poly dA:dT (1 μg/ml) for 12 h and 24 h or (K) IFN-β (500 ng/ml) for 8 h and 12 h or (L) cGAMP (1 μg/ml) for 12 h and 24 h and the supernatant was subjected to luciferase reporter assay using QuantiLuc reagent
(e) The protein expression trajectories of two representative p53 target genes showing the mRNA and protein dynamics indicated at the left were modeled for the indicated values of kdprot. Pink box shows the value of kdprot that best fits the experimentally measured protein dynamics. Cyan box shows protein expression at high kpprot.
Phenotype of the WT and ubp12i/ubp13 double mutant grown on DEX medium in the presence of increasing concentrations of BL in the light for 6 days. Scale bars: 10 mm.   Hypocotyl length relative to the mock control of seedlings (B). Experiments were done in triplicate (n >15 seedlings for each line).
D-F Serum levels of free fatty acids (FAA), insulin, and leptin in WT and KO after 25 weeks on NC or HFD (males, n=8-10). Data information: values shown are mean ±SD. * = p < 0.05; ** = p < 0.01; *** = p < 0.001; **** = p < 0.0001 (two-way ANOVA with multiple comparisons).
(F-H) Expression of LGG-1 in epg-7 mutant embryos before the ∼100-cell stage (F), at the ∼200-cell stage (G), and at the fourfold stage (H). Images in B-D and F-H were taken using the same exposure time.
(K) HeLa cells were transfected as in (C) and loaded with transferrin Alexa-647 for 30 min. Histogram and the inserts show the correlation between ATG16L1 and the loaded transferrin (Pearson's coefficient). Error bar, SEM. ∗∗∗p < 0.001.
(B) Macrophages were infected with HIVNL(AD8) or HIVNL(AD8) ΔNef. At 1, 3, 5, 7, and 10 days post-infection cells were harvested, lysed, fractionated for cytoplasmic and nuclear content, and analyzed for TFEB, ACTB and H3 histone by Western blotting. Left, representative blots are shown. Right, densitometric analysis of immunoblots from independent donors presented as means ± s.e.m., n = 4.
C, D. Men1 knock out (KO) in PIME cells through Cre-mediated gene editing upregulated Pbk protein level (C) and mRNA level (D). qPCR data was from three independent experimets (n=3).**P = 0.0059 (two-tailed unpaired student's t-test).
A. HEK293 cells treated with non-targeting (Ctrl) or C9orf72 siRNA were transfected with HA-ULK1, Myc-Rab1a or HA-ULK1+Myc-Rab1a as indicated. Transfections were laced with mVenus to enable identification of transfected cells for analysis (green). Transfected cells were probed with anti-HA and anti-Myc antibodies and processed for PLA. PLA proximity signals (red) per cell were determined from 3 independent experiments (Mean ± SEM; one-way ANOVA with Fisher's LSD test, **** P ≤ 0.0001); N (cells) = Ctrl/HA-ULK1: 125, Ctrl/Myc-Rab1a: 149, Ctrl/HA-ULK1+Myc-Rab1a: 163, C9orf72/HA-ULK1: 136, C9orf72/Myc-Rab1a: 133, C9orf72/HA-ULK1+Myc-Rab1a: 155). Scale bar = 20µm.
E. Real-time PCR analysis of IFN-β mRNA expression in peritoneal macrophages from RKIP+/+ and RKIP-/- chimera mice 12 hours after intraperitoneally injected with VSV (1x107 pfu/g) (n = 6 per group).
(C and D) qRT-PCR analysis of defense-related genes in 10-day-old seedlings exposed to 0.5 µM Pep2 for 10 h. Data are averages (±SD) of three biological replicates. (*, p < 0.05 in two-tailed tests compared to the corresponding bak1-4 and bak1-3 values in C and D, respectively. Relative cycle threshold (Ct) values of two independent experiments were combined for statistical analysis.)
C. Overexpression of MavC but not MavCC74A affects intracellular growth of the ∆mavC∆mvcA mutant of L. pneumophila. Raw264.7 cells were infected with the indicated bacterial strains and intracellular bacteria were determined at the indicated time points. Each strain was examined in triplicate and the values shown were mean +/- SE. Similar results were obtained in two independent experiments. *, p<0.1; **, p<0.01; ***, p<0.001(t-test by comparing p(MavC) with p(MavCC74A)).
(D) GST-SLBP, GST-UAP56 and GST were used for pull-down of purified MBP-ALYREF or MBP in the presence of RNase A. Proteins pulled down were separated by SDS-PAGE, followed by coomassie staining. 37.5% of input proteins were loaded.
D. Average duration (msec) of each syllable in YFO and AFO. Data information: Data are presented in the box plot or pie chart format. The central band in each box represents the median; boxes indicate the middle quartiles, and whiskers extend to the minimum and maximum values. *p<0.05, determined using Student's or Welch t-test.
(C) Alignment of PB1-F2 sequence from two avian IAV strains (VN (H5N1) and Sha (H7N9)) and two mammalian/human IAV strains (PR8 (H1N1) and Wyo (H3N2)) (Combet et al., 2000). * above the sequence shows a conserved amino acid between the four strains while ↑ on the bottom shows a different amino acid for PR8 in comparison to the other strains.
F, G. Endogenous Rabl2Q80L entered ciliary shaft to repress the export of the BBSome (Bbs5) and its cargo GPCR (Smo). mEPCs cultured from Rabl2KI/KI and wildtype neonatal mice were fixed at day 7 post serum starvation. Anti-Rabl2 antibody was used to visualize Rabl2 and Rabl2Q80L. Ac-tub or Arl13b served as ciliary marker. Representative micrographs of multicilia (F) and primary cilia (G) are shown. The white arrows point to positions of cilia.
G qRT-PCR and Western blotting analysis of Hk2, Pkm2, and Ldha in WT and miR‐290 cluster−/−ESCs.
(C, D) Internalized BACE1 levels after 20 min of HA antibody pulse in HA-BACE1-eGFP-overexpressing WT and KO neurons, calculated as the HA (internalized)/eGFP (total) signal intensity ratio (WT: 0.50±0.052, KO: 0.23±0.036, p=0.000, 30 WT and 36 KO neurons, N=4 biological replicates). Scale bar: 5 µm. Data information: Experimental designs are depicted in the top panels where analyzed BACE1 fraction is marked with the red square. All graphs show mean ± SEM, statistical analysis was performed by unpaired two-tailed Student's t‐test n.s.-non-significant. * indicates p≤0.05, ** indicates p≤0.01, *** indicates p≤0.001.
C Tumor growth curves in tumor-bearing WT and KO mice treated with PBS or anti-mouse IL-6 antibody (n=5).
E. Quantification of endocytosis-rescue experiments in HeLa cells. HeLaVPS41KO cells transfected with VPS41WT-APEX2-V5 show a significant increase in colocalization of endocytosed Dextran-568 and SiR-Lysosome Cathepsin D (SiR-Lyso), indicating rescue of the endocytosis phenotype. Neither VPS41 variant rescues this HOPS complex functionality. >13 Cells per cell line per experiment were quantified (n=3).
A. H295R/TR N-FlagFATE1 cells were transfected with D1 ER marker for ER (green) and mtRFP marker for mitochondria (red). Manders' coefficient for green-red signals colocalization in basal (white histograms) and Dox-treated (black histograms) cells is shown on the right (mean ± SEM; n=12). ***p<0.001. Scale bars, 10 μm.
Schematic model of the HA-tagged constitutively active Akt form targeted to the mitochondrial intermembrane space (mt-Akt D/D). Both the expression and the mitochondrial localization of the chimera were assessed by immunofluorescence. TOM20 was used as a mitochondrial marker. Merged images are indicated (merge). Scale bar 10 μm
(E) Immunoprecipitation of HA-tagged EBNA2 mutant ST266AV, TSS377VAA and SPSS467APAA using HA-specific antibodies.
(h) ELISA for IL-1β in supernatants. Resting or LPS-primed BMMs generated from WT or Casp1-/- mice were stimulated with PA-BSA, BSA control, ATP or nigericin.
C. Confocal images of control and NPC1I1061T patient fibroblasts expressing ARF1-GFP. Insets show enlarged views of ARF1 in the Golgi area. Tubular structures were observed in NPC1I1061T patient fibroblasts as indicated by the black arrows. D. Quantification of ΑRF-1 fluorescence intensity in Golgi normalized to the cytoplasm in control and NPC1I1061T patient fibroblasts. Control: n=10; NPC1I1061T: n=11.
In vitro phosphorylation analysis of Rab8A by PINK1. WT or S111A‐mutant Rab8A (1.2 μg) was incubated in the presence of MBP‐fused WT or KI (D359A) TcPINK1 (1.1 μg) and Mg2+‐[γ‐32P] ATP for the indicated time. Samples were subjected to SDS-PAGE, and proteins were detected by colloidal Coomassie blue staining (lower panel). The [γ‐32P] incorporation to substrate was detected by autoradiography (upper panel). Cerenkov counting was used to calculate the stoichiometry of substrate phosphorylation as mol of [γ‐32P] incorporation/mol of substrate. Ubiquitin was used as a positive control of the TcPINK1 substrate.
25HC inhibits membrane fusion mediated by , SARS-CoV S (G, left), and MERS-CoV S (G, right). 293FT or Vero cells were treated with EtOH or 25HC (5 µM) for 16h prior to transfection with pLVX plasmids encoding , SARS-CoV S (G, left), and MERS-CoV S (G, right) in the absence of EtOH or 25HC. At 24h post-transfection, syncytium formation was visualized by fluorescence microscopy. Scale bar, 50 μm. White arrows indicate syncytia. Quantification of membrane fusion was performed by calculating the percentages of nuclei involved in syncytia formation from all nuclei in GFP positive cells.
(A-B) RNAPII occupancy on chromatin in S phase was assessed by ChIP-qPCR. (A) The level of Rpb1 was measured at snR13-TRS31 in both G1 and S phase (70 min at 16°C). Data is expressed as a percentage of input. SEM (n=3 biological replicates) is indicated. (B) Quantification of the data from (A) depicting the mean retention of Rpb1 in S phase over G1.
(A) Western blot on whole cell extracts and chromatin fractions extracted from kidneys of WT males and ARLmon/Y mice. Antibodies against GAPDH and Histone 3 were used to confirm cellular fractionation. Relative intensities are indicated, whereby the upper bands (AR) are normalized to the lower bands (GAPDH or Histone 3). Both panels represent the same blot. The blot was cut in two parts and a longer exposure time was used for AR visualization (upper panel).
(C) Co-immunoprecipitation and immunoblot analysis of extracts of 293T cells transfected with Flag-caspase-1 (WT or K134R) and HA-K11-Ub, together with empty vector or Myc-NS1. Lower panel shows the intensity analysis of the bands from the three independent experiments.
Eight-week-old male WT and DOCK5-/- mice were fed a standard diet (SD) or high-fat diet ( HFD) for 3 months. Average daily food intake.
(C and D) The axons passing through the ROI was quantified by measuring the fluorescence intensity in the ROI, and the distribution of axons was statistically analyzed (n = 5; t-test; **P < 0.005)
respirometry analysis (C in C2C12 myocytes transfected with siRNA or plasmid for mGPDH 24 h after differentiation
(D) Failure of truncated MAKR5 fusion proteins to complement CLE45 insensitivity of the makr5 mutant (7-day-old seedlings; 1-2 independent transgenic lines per construct are shown).
Histologic assessment of p129-SNCA immunoreactivity ( I,J), TH+ mDA neuron counts (I,K), neurite lengths (L), and cell body sizes (M) in the SN Significantly different at p=0.0001* in graph J, p=2.35E-25#, 1.09E-16##, 4.36E-08* in graph K and p=1.5E-40#, 1.08E-24##, 2.32E-07* in graph L and p=9.07E-20#, 2.59E-16##, 0.05* in graph M and p=4.62E-22#, 5.11E-12##, 3.49E-06* (TH), n= 7 sh-SGK1-AAV9-treated PD mice, 7 sh-cont-AAV9-treated PD mice, and 8 SNCA-untreated mice. Data are represented as mean ± SEM. One-way ANOVA. Scale bar, 100µm.
(A) p47 requires its association with FTCD for its localization to the Golgi at the end of mitosis. HepG2 cells were treated with FTCD siRNA and then the indicated HA-tagged FTCDs were expressed as described in Figure 4C. The mitotic cells were collected, cultured for 35 mins, and then fixed. The cells were stained with polyclonal antibodies to p47 and HA and a monoclonal antibody to GM130, and observed by confocal microscopy. Panels a-l show the distribution of p47 or/and GM130 and panels m-o show HA-FTCD expression. Scale bar = 10 μm. (B) Insets in (A). p47 (red) and the GM130 (a Golgi marker, green) were visualized. Scale bar = 5 μm. (C) The results of quantification of (A). The results are shown as the mean±SD of five sets of independent experiments, with 100 cells counted in each group in each independent experiments. Asterisks indicate a significant difference at P<0.01 compared with the mock-treated cells (Bonferroni method).
F The effect of HSATIII knockdown on time course-dependent changes in SRSF9 phosphorylation. The phosphorylation states were estimated by Phos-tag SDS-PAGE, followed by western blotting using an anti-SRSF9 antibody. SRSF9 detected by western blotting of a normal SDS-PAGE gel is shown in the bottom panel. The arrows and arrowheads indicate the normal phosphorylated forms and thermal stress-induced hypo- and de-phosphorylated forms, respectively. G Quantification of the data shown in (F). Graphs show the time-course changes in four representative SRSF9 phosphorylated forms in (F). Relative levels of band intensity were calculated as the ratio of each band to α-tubulin and were normalized to those of control at 37°C (bands (a) and (b)) and 42°C (bands (c) and (d)). Since band (d) partially overlapped with the other band (asterisk in (F)) at 37°C and recovery 4h, band (d) at those time points was not measured.
Representative IF-images showing Rad51 foci in S-phase (Edu positive) U2OS nucleus after 5h of IR (2Gy) exposure. (Scale bar; 10µm).   Graph represents the quantification of (E) showing average number of Rad51 foci per S-phase (Edu positive) nucleus. (ns P>0.05, ****P<0.0001; unpaired t-test, n=2, mean +SEM, at least 50 nuclei per condition and experiment).
A: Chromatogram and SDS-PAGE analysis of elution fractions from analytical size exclusion chromatography. Dam1c and Bim1 individually or in combination were subjected to gel filtration. Bim1 coelutes with Dam1c and forms a stoichiometric complex.
(A) Sections from the cerebellar vermis of a 70-d-old npc1−/− mouse were stained with anti-Calbindin (green) to visualize PCs and 7AAD (red) for nuclei. Although there are scant PCs remaining in lobule II, the PCs in lobule X have not decreased.
g, Samples from drpr null animals (+/w; +/UAS-Drpr-I; drpr∆5/drpr∆5), n = 9, and those with salivary gland-specific expression of Drpr-I (fkh-Gal4/w; UAS-Drpr-I/+; drpr∆5/drpr∆5), n = 20, analysed by histology for the presence of salivary gland material (red circles) 24 h after puparium formation. h, Quantification of data from g.
Stacked bar plot (Marimekko chart) representation of macrophage subsets to a given cluster demonstrating pure microglia populations in clusters 13, 14 and 15. Hypergeometric testing revealed significantly enriched macrophage clusters in the cornea (2, 3, 6, 9, 16) and the ciliary body (1, 5, 10, 11, 12) as indicated by asterisks (*p < 0.05, **p < 0.01, ***p < 0.001).
(b) Summary of rod and cone death kinetics. Time is indicated in postnatal days or weeks. (c) Immunofluorescence microscopy on retinal flat mounts showing the ventral reduction of red/green opsin expression found in the four mutants during cone degeneration. Strain and time, in postnatal days, are indicated below each image (for higher magnification of wild type, see Fig. 2b).
H Quantification of parasite with DHHC2 polarization in P28 positive cells. Parasites are indicated in (G) or from a genetic cross (dhhc2::6HA/cdpk4 and WT). x/y: the number of cells with DHHC2 polarization and the number of cells analyzed. Values are means ± SD from three tests, two-tailed t test, ***, P<0.001, ****, P<0.0001, ns, not significant.
Oil Red O staining and enzymatic activity of respiratory CI in transverse contiguous slices (R). Images are representative of n= 4 mice/genotype, 10 images/mouse. Note the colocalization of oxidative fibers with LDs (R).
Skin tumor outcomes in WT mice treated with DMBA/TPA carcinogenesis protocol in combination with SB431542 (test, n=9) or acetone (carrier control, n=5). (D) skin tumor volume at the completion of the DMBA/TPA carcinogenesis protocol.
Binding mode of the LARP6-RRM domain with Bumetanide. The protein is shown as cartoons and is green. Bumetanide and dominant residues are shown as sticks. Bumetanide is cyan and the dominant residues are green.
I. pICLpt was replicated in egg extracts immunodepleted with the indicated antibodies and processed as in Figure 3J,L.
D. Schematic representation of the LYS2 locus with primers located at 1 kb from the I-SceI site for the DNA measurements (blue arrows).