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PROSITE documentation PDOC51319 [for PROSITE entry PS51319]

TFIIS N-terminal domain profile





Description

Transcription factor IIS (TFIIS) is a transcription elongation factor that increases the overall transcription rate of RNA polymerase II by reactivating transcription elongation complexes that have arrested transcription. The three structural domains of TFIIS are conserved from yeast to human. The 80 or so N-terminal residues form a protein interaction domain containing a conserved motif, which has been called the LW motif because of the invariant leucine and tryptophane residues it contains. Although the N-terminal domain is not needed for transcriptional activity, a similar sequence has been identified in other transcription factors and proteins that are predominantly nuclear localized [1,2]:

  • MED26 (also known as CRSP70 and ARC70), a subunit of the Mediator complex, which is required for the activity of the enhancer-binding protein Sp1.
  • Elongin A, a subunit of a transcription elongation factor previously known as SIII. It increases the rate of transcription by suppressing transient pausing of the elongation complex.
  • PPP1R10, a nuclear regulatory subunit of protein phosphatase 1 that was previously known as p99, FB19 or PNUTS.
  • PIBP, a small hypothetical protein that could be a phosphoinositide binding protein.
  • IWS1, which is thought to function in both transcription initiation and elongation.

The TFIIS N-terminal domain is a compact four-helix bundle (see <PDB:1EO0>). The hydrophobic core residues of helices 2, 3, and 4 are well conserved among TFIIS domains, although helix 1 is less conserved [2].

The profile we developed covers the entire TFIIS N-terminal domain.

Last update:

June 2007 / First entry.

Technical section

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

TFIIS_N, PS51319; TFIIS N-terminal domain profile  (MATRIX)


References

1AuthorsBooth V. Koth C.M. Edwards A.M. Arrowsmith C.H.
TitleStructure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70.
SourceJ. Biol. Chem. 275:31266-31268(2000).
PubMed ID10811649
DOI10.1074/jbc.M002595200

2AuthorsLing Y. Smith A.J. Morgan G.T.
TitleA sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIIS.
SourceNucleic Acids Res. 34:2219-2229(2006).
PubMed ID16648364
DOI10.1093/nar/gkl239



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Miscellaneous

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