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17  structures 337  species 0  interactions 1989  sequences 26  architectures

Family: HSF_DNA-bind (PF00447)

Summary: HSF-type DNA-binding

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This is the Wikipedia entry entitled "Heat shock factor". More...

Heat shock factor Edit Wikipedia article

HSF-type DNA-binding
Heat shock factor 3HTS.png
Structure of the dimeric DNA binding domain of the yeast heat shock factor (cyan and green) bound to DNA (brown) based on PDB 3HTS.
Identifiers
Symbol HSF_DNA-bind
Pfam PF00447
InterPro IPR000232
PROSITE PDOC00381
SCOP 1hks
SUPERFAMILY 1hks
Vertebrate heat shock transcription factor
Identifiers
Symbol Vert_HS_TF
Pfam PF06546
InterPro IPR010542

Heat shock factor (HSF), in molecular biology, is the name given to transcription factors that regulate the expression of the heat shock proteins.[1][2] A typical example is the heat shock factor of Drosophila melanogaster.[3]

Function[edit]

Heat shock factors (HSF) are transcriptional activators of heat shock genes.[3] These activators bind specifically to Heat Shock sequence Elements (HSE) throughout the genome[4] whose consensus-sequence is a tandem array of three oppositely oriented "AGAAN" motifs or a degenerate version thereof. Under non-stressed conditions, Drosophila HSF is a nuclear-localized unbound monomer, whereas heat shock activation results in trimerization and binding to the HSE.[5] The Heat Shock sequence Element is highly conserved from yeast to humans.[6]

Heat shock factor 1 (HSF-1) is the major regulator of heat shock protein transcription in eukaryotes. In the absence of cellular stress, HSF-1 is inhibited by association with heat shock proteins and is therefore not active. Cellular stresses, such as increased temperature, can cause proteins in the cell to misfold. Heat shock proteins bind to the misfolded proteins and dissociate from HSF-1. This allows HSF1 to form trimers and translocate to the cell nucleus and activate transcription.[7]

Structure[edit]

Each HSF monomer contains one C-terminal and three N-terminal leucine zipper repeats.[8] Point mutations in these regions result in disruption of cellular localisation, rendering the protein constitutively nuclear in humans.[5] Two sequences flanking the N-terminal zippers fit the consensus of a bi-partite nuclear localization signal (NLS). Interaction between the N- and C-terminal zippers may result in a structure that masks the NLS sequences: following activation of HSF, these may then be unmasked, resulting in relocalisation of the protein to the nucleus.[8] The DNA-binding component of HSF lies to the N-terminus of the first NLS region, and is referred to as the HSF domain.

Isoforms[edit]

Humans express the following heat shock factors:

gene protein
HSF1 heat shock transcription factor 1
HSF2 heat shock transcription factor 2
HSF2BP heat shock transcription factor 2 binding protein
HSF4 heat shock transcription factor 4
HSF5 heat shock transcription factor family member 5
HSFX1 heat shock transcription factor family, X linked 1
HSFX2 heat shock transcription factor family, X linked 2
HSFY1 heat shock transcription factor, Y-linked 1
HSFY2 heat shock transcription factor, Y-linked 2

References[edit]

  1. ^ Sorger PK (May 1991). "Heat shock factor and the heat shock response". Cell 65 (3): 363–6. doi:10.1016/0092-8674(91)90452-5. PMID 2018972. 
  2. ^ Morimoto RI (March 1993). "Cells in stress: transcriptional activation of heat shock genes". Science 259 (5100): 1409–10. doi:10.1126/science.8451637. PMID 8451637. 
  3. ^ a b Clos J, Westwood JT, Becker PB, Wilson S, Lambert K, Wu C (November 1990). "Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation". Cell 63 (5): 1085–97. doi:10.1016/0092-8674(90)90511-C. PMID 2257625. 
  4. ^ Guertin, MJ; Lis, JT (Sep 2010). "Chromatin landscape dictates HSF binding to target DNA elements.". PLoS Genetics 6 (9). doi:10.1371/journal.pgen.1001114. PMC 2936546. PMID 20844575. 
  5. ^ a b Rabindran SK, Giorgi G, Clos J, Wu C (August 1991). "Molecular cloning and expression of a human heat shock factor, HSF1". Proc. Natl. Acad. Sci. U.S.A. 88 (16): 6906–10. doi:10.1073/pnas.88.16.6906. PMC 52202. PMID 1871105. 
  6. ^ Guertin, MJ; Petesch SJ, Zobeck KL, Min IM, Lis JT. (2010). "Drosophila heat shock system as a general model to investigate transcriptional regulation.". Cold Spring Harb Symp Quant Biol. 75: 1–9. doi:10.1101/sqb.2010.75.039. PMID 21467139. 
  7. ^ Prahlad, V, Morimoto RI (Dec 2008). "Integrating the stress response: lessons for neurodegenerative diseases from C. elegans". Trends in Cell Biology 19 (2): 52–61. doi:10.1016/j.tcb.2008.11.002. PMID 19112021. 
  8. ^ a b Schuetz TJ, Gallo GJ, Sheldon L, Tempst P, Kingston RE (August 1991). "Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans". Proc. Natl. Acad. Sci. U.S.A. 88 (16): 6911–5. doi:10.1073/pnas.88.16.6911. PMC 52203. PMID 1871106. 

This article incorporates text from the public domain Pfam and InterPro IPR000232

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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HSF-type DNA-binding Provide feedback

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Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000232

Heat shock factor (HSF) is a transcriptional activator of heat shock genes [PUBMED:2257625]: it binds specifically to heat shock promoter elements, which are palindromic sequences rich with repetitive purine and pyrimidine motifs [PUBMED:2257625]. Under normal conditions, HSF is a homo-trimeric cytoplasmic protein, but heat shock activation results in relocalisation to the nucleus [PUBMED:1871105]. Each HSF monomer contains one C-terminal and three N-terminal leucine zipper repeats [PUBMED:1871106]. Point mutations in these regions result in disruption of cellular localisation, rendering the protein constitutively nuclear [PUBMED:1871105]. Two sequences flanking the N-terminal zippers fit the consensus of a bi- partite nuclear localisation signal (NLS). Interaction between the N- and C-terminal zippers may result in a structure that masks the NLS sequences: following activation of HSF, these may then be unmasked, resulting in relocalisation of the protein to the nucleus [PUBMED:1871106]. The DNA-binding component of HSF lies to the N terminus of the first NLS region, and is referred to as the HSF domain.

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan HTH (CL0123), which has the following description:

This family contains a diverse range of mostly DNA-binding domains that contain a helix-turn-helix motif.

The clan contains the following 202 members:

AphA_like Arg_repressor B-block_TFIIIC Bac_DnaA_C BetR Bot1p BrkDBD CENP-B_N Cro Crp DDRGK Dimerisation DUF1133 DUF1153 DUF1323 DUF134 DUF1441 DUF1492 DUF1495 DUF1670 DUF1804 DUF1836 DUF1870 DUF2089 DUF2250 DUF2316 DUF3116 DUF3853 DUF387 DUF3908 DUF4095 DUF4364 DUF739 DUF742 DUF977 E2F_TDP ELK Ets Exc F-112 FaeA Fe_dep_repr_C Fe_dep_repress FeoC Ftsk_gamma FUR GcrA GerE GntR HARE-HTH HemN_C Homeobox Homeobox_KN Homez HrcA_DNA-bdg HSF_DNA-bind HTH_1 HTH_10 HTH_11 HTH_12 HTH_13 HTH_15 HTH_16 HTH_17 HTH_18 HTH_19 HTH_20 HTH_21 HTH_22 HTH_23 HTH_24 HTH_25 HTH_26 HTH_27 HTH_28 HTH_29 HTH_3 HTH_30 HTH_31 HTH_32 HTH_33 HTH_34 HTH_35 HTH_36 HTH_37 HTH_38 HTH_39 HTH_40 HTH_41 HTH_42 HTH_43 HTH_45 HTH_5 HTH_6 HTH_7 HTH_8 HTH_9 HTH_AraC HTH_AsnC-type HTH_CodY HTH_Crp_2 HTH_DeoR HTH_IclR HTH_Mga HTH_OrfB_IS605 HTH_psq HTH_Tnp_1 HTH_Tnp_1_2 HTH_Tnp_4 HTH_Tnp_IS1 HTH_Tnp_IS630 HTH_Tnp_ISL3 HTH_Tnp_Mu_1 HTH_Tnp_Mu_2 HTH_Tnp_Tc3_1 HTH_Tnp_Tc3_2 HTH_Tnp_Tc5 HTH_WhiA HxlR IF2_N KorB LacI LexA_DNA_bind LZ_Tnp_IS481 MADF_DNA_bdg MarR MarR_2 Med9 MerR MerR-DNA-bind MerR_1 MerR_2 Mga Mnd1 Mor MotA_activ MRP-L20 Myb_DNA-bind_2 Myb_DNA-bind_3 Myb_DNA-bind_4 Myb_DNA-bind_5 Myb_DNA-bind_6 Myb_DNA-binding Neugrin NUMOD1 OST-HTH P22_Cro PaaX PadR PAX PCI PCI_Csn8 Penicillinase_R Phage_AlpA Phage_antitermQ Phage_CI_repr Phage_CII Phage_rep_org_N Phage_terminase Pou Pox_D5 PuR_N Put_DNA-bind_N Rap1-DNA-bind Rep_3 RepA_C RepA_N RepC RepL Replic_Relax RFX_DNA_binding Ribosomal_S25 Rio2_N RNA_pol_Rpc34 RP-C RPA RPA_C RQC Rrf2 RTP SAC3_GANP SgrR_N Sigma54_CBD Sigma54_DBD Sigma70_ECF Sigma70_r2 Sigma70_r3 Sigma70_r4 Sigma70_r4_2 SpoIIID Sulfolobus_pRN TBPIP Terminase_5 TetR_N TFIIE_alpha Tn916-Xis Trans_reg_C TrfA TrmB Trp_repressor UPF0122 z-alpha

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(114)
Full
(1989)
Representative proteomes NCBI
(1973)
Meta
(19)
RP15
(519)
RP35
(792)
RP55
(1058)
RP75
(1305)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(114)
Full
(1989)
Representative proteomes NCBI
(1973)
Meta
(19)
RP15
(519)
RP35
(792)
RP55
(1058)
RP75
(1305)
Alignment:
Format:
Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(114)
Full
(1989)
Representative proteomes NCBI
(1973)
Meta
(19)
RP15
(519)
RP35
(792)
RP55
(1058)
RP75
(1305)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Family
Author: Finn RD
Number in seed: 114
Number in full: 1989
Average length of the domain: 99.60 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 21.34 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 21.0
Trusted cut-off 21.0 21.0
Noise cut-off 20.9 20.6
Model length: 104
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HSF_DNA-bind domain has been found. There are 17 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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