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PROSITE documentation PDOC51526

RFX-type winged-helix DNA-binding domain profile





Description

The RFX family of transcription factors is characterized by a unique ~75-residue DNA-binding domain. RFX genes have been isolated in yeasts, nematode and vertebrates. The characteristic RFX-type HTH DNA binding domain has been recruited into otherwise very divergent regulatory factors functioning in a diverse spectrum of unrelated systems, including regulation of the mitotic cell cycle in fission yeast, the control of the immune response in mammals, and infection by human hepatitis B virus [1,2].

The RFX-type DNA-binding domain is an unusual member of the winged-helix subfamily of helix-turn-helix domains because it uses a β-hairpin (or wing) to recognize DNA instead of the recognition helix typical of helix-tun-helix domains. It consists of three α-helices (H), three β-strands (S) and three connecting loops (L), arranged in the order H1-S1-H2-L1-H3-L2-S2-W1-S3. The third loop, connecting β-strands S2 and S3, forms wing W1 of the winged-helix motif (see <PDB:1DP7>). In contrast to previously described winged-helix DBDs (typically 110 residues long with two wings, W1 and W2), the shorter RFX-type winged-helix DNA-binding domain has only one wing [3].

Some proteins known to contain a RFX-type winged-helix DNA-binding domain are listed below:

  • Human RFX1, a cellular transactivator that is used by the highly pathogenic hepatitis B virus.
  • Human RFX2.
  • Human RFX3, a transcription factor required for ciliogenesis and islet cell differentiation during endocrine pancreas development.
  • Human RFX5, a regulator of MHC class II gene transcription.
  • Human ARID2, a component of the SWI/SNF-B (PBAF) chromatin remodeling complex [4].
  • Yeast Crt1, an effector of the DNA damage and replication checkpoint.
  • Schizosaccharomyces pombe sak1, an essential regulatory protein in the life cycle. It allows cells to exit the mitotic cycle and enter either the stationary phase or the pathway leading to sexual differentiation.

The profile we developed covers the entire RFX-type winged-helix DNA-binding domain.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

March 2011 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

RFX_DBD, PS51526; RFX-type winged-helix DNA-binding domain profile  (MATRIX)


References

1AuthorsEmery P. Durand B. Mach B. Reith W.
TitleRFX proteins, a novel family of DNA binding proteins conserved in the eukaryotic kingdom.
SourceNucleic Acids Res. 24:803-807(1996).
PubMed ID8600444

2AuthorsDurand B. Vandaele C. Spencer D. Pantalacci S. Couble P.
TitleCloning and characterization of dRFX, the Drosophila member of the RFX family of transcription factors.
SourceGene 246:285-293(2000).
PubMed ID10767550

3AuthorsGajiwala K.S. Chen H. Cornille F. Roques B.P. Reith W. Mach B. Burley S.K.
TitleStructure of the winged-helix protein hRFX1 reveals a new mode of DNA binding.
SourceNature 403:916-921(2000).
PubMed ID10706293
DOI10.1038/35002634

4AuthorsPatsialou A. Wilsker D. Moran E.
TitleDNA-binding properties of ARID family proteins.
SourceNucleic Acids Res. 33:66-80(2005).
PubMed ID15640446
DOI10.1093/nar/gki145



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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