PROSITE documentation PDOC51321 [for PROSITE entry PS51321]TFIIS central domain profile
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.
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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). | |
| PubMed ID | 8855225 |
| 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). | |
| PubMed ID | 9712887 |
| 3 | Authors | Kettenberger H. Armache K.-J. Cramer P. |
| Title | Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. | |
| Source | Cell 114:347-357(2003). | |
| PubMed ID | 12914699 |
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