This entry represents transcription elongation factors of the IIS type. TFIIS is a component of RNA polymerase II preinitiation complexes, and is required for preinitiation complex assembly and stability [1]. The association of TFIIS with a promoter depends on functional preinitiation complex components including Mediator and the SAGA complex [2]. TFIIS is composed of three domains: domain 1 forms a 4-helical bundle that appears to bind certain initiation factors; domain 2 forms a 3-helical bundle and is required for Pol II binding; domain 3 forms a zinc ribbon and is essential for stimulation of RNA cleavage [3, 4].

1. The transcription elongation factor TFIIS is a component of RNA polymerase II preinitiation complexes. Proc. Natl. Acad. Sci. U.S.A. 104, 16068-73
2. TFIIS elongation factor and Mediator act in conjunction during transcription initiation in vivo. Proc. Natl. Acad. Sci. U.S.A. 104, 16062-7
3. A sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIIS. Nucleic Acids Res. 34, 2219-29
4. Structural basis for the species-specific activity of TFIIS. J. Biol. Chem. 275, 36541-9

This entry represents transcription elongation factors of the IIS type. TFIIS is a component of R
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