Structural highlights
Function
[T2EB_HUMAN] Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human general transcription factor TFIIE consists of two subunits, TFIIEalpha and TFIIEbeta. Recently, TFIIEbeta has been found to bind to the region where the promoter starts to open to be single-stranded upon transcription initiation by RNA polymerase II. Here, the central core domain of human TFIIEbeta (TFIIEbetac) has been identified by a limited proteolysis. This solution structure has been determined by NMR. It consists of three helices with a beta hairpin at the C-terminus, resembling the winged helix proteins. However, TFIIEbetac shows a novel double-stranded DNA-binding activity where the DNA-binding surface locates on the opposite side to the previously reported winged helix motif by forming a positively charged furrow. A model will be proposed that TFIIE stabilizes the preinitiation complex by binding not only to the general transcription factors together with RNA polymerase II but also to the promoter DNA, where double-stranded DNA starts to open to be single-stranded upon activation of the preinitiation complex.
Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface.,Okuda M, Watanabe Y, Okamura H, Hanaoka F, Ohkuma Y, Nishimura Y EMBO J. 2000 Mar 15;19(6):1346-56. PMID:10716934[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Okuda M, Watanabe Y, Okamura H, Hanaoka F, Ohkuma Y, Nishimura Y. Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface. EMBO J. 2000 Mar 15;19(6):1346-56. PMID:10716934 doi:10.1093/emboj/19.6.1346
