Protein: Heat shock transcription factor hsf-1 (G5EFT5)
Organism: Caenorhabditis elegans
Function: Functions as a stress-inducible and DNA-binding transcription factor, playing a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage. Upon exposure to heat and other stress stimuli, activates gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of target genes, such as the HSPs. Binds to inverted 5'-NGAAN-3' pentamer DNA sequences in HSEs. Involved in positive modulation of expression of heat shock protein hsp-16.2 in response to heat shock; may act in concert with homeodomain-interacting protein kinase hpk-1. In response to heat shock or starvation, required for the modulation of lifespan, and protection against aberrant protein aggregation proteotoxicity; may act in parallel with the Insulin/IGF-1-like signaling (IIS) mediated pathway. Plays a role in modulating autophagy, in response to a moderate and short-term heat shock, also known as a hormetic heat shock. Involved in positive modulation of ascaroside pheromone biosynthesis in response to heat shock, perhaps by directly activating transcription of peroxisomal fatty acid beta-oxidation genes. Required in modulating the response to infection by either Gram-negative or Gram-positive bacteria, perhaps acting via regulation of expression of Hsp90/daf-21 and members of the small heat shock protein (HSP20) family. May play a role downstream of the daf-16/FOXO and daf-2 signaling pathway in response to bacterial pathogens. Modulates expression of multiple microRNA genes, in both heat shock-dependent and -independent manner. Independent of heat shock, required to modulate expression of genes involved in larval development, mainly distinct from HSPs; acts in concert with putative transcription factor efl-1/E2F, which may form part of a multiprotein DRM complex. Independent of heat shock, involved in promoting death of the linker cell, a male-specific cell which guides the elongation of the gonad; perhaps acting by modulating expression of ubiquitin-conjugating enzyme let-70. Plays a role in egg-laying.
Subcellular location: Nucleus {ECO:0000269|PubMed:23107491}. Cytoplasm {ECO:0000269|PubMed:22265419}. Note=Localizes constitutively to the nucleus (PubMed:23107491, PubMed:29042483). Localization to the nucleus enhanced by heat shock (PubMed:22265419). Localization to nucleus inhibited by the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:22265419). In response to heat shock, forms nuclear stress granules (PubMed:23107491, PubMed:29036198). These structures are dependent upon either heat shock, or can be induced by treatment with sodium azide, which may act by inhibiting ATP production (PubMed:23107491). DNA binding may promote localization to stress granules (PubMed:23107491). Localization to stress granules partially overlaps with sites of active transcription (PubMed:23107491). Other stressors such as osmotic stress, heavy metals, or ethanol do not induce localization to nuclear stress granules (PubMed:23107491). {ECO:0000269|PubMed:22265419, ECO:0000269|PubMed:23107491, ECO:0000269|PubMed:29036198, ECO:0000269|PubMed:29042483}.
Interaction partners:
- Heat shock protein 90
- WASH complex subunit homolog 3
- Heat shock factor-binding protein 1
- Heat shock protein hsp-16.2
- Forkhead box protein O
- WASH complex subunit homolog 1
- Heat shock protein 70
- Protein skinhead-1
- Insulin-like receptor
- Heat shock protein Hsp-16.1/Hsp-16.11
Sequence:
MQPTGNQIQQNQQQQQQLIMRVPKQEVSVSGAARRYVQQAPPNRPPRQNHQNGAIGGKKSSVTIQEVPNNAYLETLNKSGNNKVDDDKLPVFLIKLWNIVEDPNLQSIVHWDDSGASFHISDPYLFGRNVLPHFFKHNNMNSMVRQLNMYGFRKMTPLSQGGLTRTESDQDHLEFSHPCFVQGRPELLSQIKRKQSARTVEDKQVNEQTQQNLEVVMAEMRAMREKAKNMEDKMNKLTKENRDMWTQMGSMRQQHARQQQYFKKLLHFLVSVMQPGLSKRVAKRGVLEIDFCAANGTAGPNSKRARMNSEEGPYKDVCDLLESLQRETQEPFSRRFTNNEGPLISEVTDEFGNSPVGRGSAQDLFGDTFGAQSSRYSDGGATSSREQSPHPIISQPQSNSAGAHGANEQKPDDMYMGSGPLTHENIHRGISALKRDYQGASPASGGPSTSSSAPSGAGAGARMAQKRAAPYKNATRQMAQPQQDYSGGFVNNYSGFMPSDPSMIPYQPSHQYLQPHQKLMAIEDQHHPTTSTSSTNADPHQNLYSPTLGLSPSFDRQLSQELQEYFTGTDTSLESFRDLVSNHNWDDFGNNVPLDDDEEGSEDPLRQLALENAPETSNYDGAEDLLFDNEQQYPENGFDVPDPNYLPLADEEIFPHSPALRTPSPSDPNLV