|PROSITE documentation PDOC51321 [for PROSITE entry PS51321]|
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  (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 . The TFIIS domain is separated from the TFIIS-type zinc finger by an interdomain linker , which is unstructured in free TFIIs . Upon Pol II binding, however, the linker forms an α-helix, which runs along the Pol II bottom face .
The profile we developed covers the TFIIS central domain and the linker α-helix.Last update:
June 2007 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Morin P.E. Awrey D.E. Edwards A.M. Arrowsmith C.H.|
|Title||Elongation factor TFIIS contains three structural domains: solution structure of domain II.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 93:10604-10608(1996).|
|2||Authors||Olmsted V.K. Awrey D.E. Koth C. Shan X. Morin P.E. Kazanis S. Edwards A.M. Arrowsmith C.H.|
|Title||Yeast transcript elongation factor (TFIIS), structure and function. I: NMR structural analysis of the minimal transcriptionally active region.|
|Source||J. Biol. Chem. 273:22589-22594(1998).|
|3||Authors||Kettenberger H. Armache K.-J. Cramer P.|
|Title||Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage.|