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PROSITE documentation PDOC51321 [for PROSITE entry PS51321]

TFIIS central 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. TFIIS is a modular factor that comprises an N-terminal domain (see <PDOC51319>), a central domain, and a C-terminal TFIIS-type zinc finger (see <PDOC00383>). The central domain is conserved in TFIIS homologues and interacts with RNA polymerase II [1,2].

The TFIIS central domain comprises a bundle of three helices [1,2] and three short helices, which form upon Pol II interaction [3] (see <PDB:1PQV>). The three-helix bundle is built around a hydrophobic core composed largely of three tyrosines protruding from one face of the C-terminal helix [1]. The TFIIS domain is separated from the TFIIS-type zinc finger by an interdomain linker [1], which is unstructured in free TFIIs [2]. Upon Pol II binding, however, the linker forms an α-helix, which runs along the Pol II bottom face [3].

The profile we developed covers the TFIIS central domain and the linker α-helix.

Last update:

June 2007 / First entry.

Technical section

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

TFIIS_CENTRAL, PS51321; TFIIS central domain profile  (MATRIX)


References

1AuthorsMorin P.E. Awrey D.E. Edwards A.M. Arrowsmith C.H.
TitleElongation factor TFIIS contains three structural domains: solution structure of domain II.
SourceProc. Natl. Acad. Sci. U.S.A. 93:10604-10608(1996).
PubMed ID8855225

2AuthorsOlmsted V.K. Awrey D.E. Koth C. Shan X. Morin P.E. Kazanis S. Edwards A.M. Arrowsmith C.H.
TitleYeast transcript elongation factor (TFIIS), structure and function. I: NMR structural analysis of the minimal transcriptionally active region.
SourceJ. Biol. Chem. 273:22589-22594(1998).
PubMed ID9712887

3AuthorsKettenberger H. Armache K.-J. Cramer P.
TitleArchitecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage.
SourceCell 114:347-357(2003).
PubMed ID12914699



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