|PROSITE documentation PDOC51319 [for PROSITE entry PS51319]|
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]:
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 .
The profile we developed covers the entire TFIIS N-terminal domain.Last update:
June 2007 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Booth V. Koth C.M. Edwards A.M. Arrowsmith C.H.|
|Title||Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70.|
|Source||J. Biol. Chem. 275:31266-31268(2000).|
|2||Authors||Ling Y. Smith A.J. Morgan G.T.|
|Title||A sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIIS.|
|Source||Nucleic Acids Res. 34:2219-2229(2006).|