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Structure and oligomeric state of human transcription factor TFIIE
Structure and oligomeric state of human transcription factor TFIIE
7335
The general RNA polymerase II transcription factor TFIIE, which is composed of two subunits, has essential roles in both transcription initiation and promoter escape. Electron microscopy analysis of negatively stained human TFIIE showed a large proportion of alpha/beta heterodimers as well as a small proportion of tetramers. Analytical ultracentrifugation, chemical crosslinking, pulldown experiments and cryo-electron microscopy confirmed that TFIIE is a alpha/beta heterodimer in solution. Three-dimensional envelopes of the alpha/beta particles showed an elongated structure composed of three distinct modules. Finally, a model for the quaternary architecture of the complex is proposed that provides a structural framework to discuss the function of TFIIE in the context of RNA polymerase II transcription initiation.
Jawhari A, Uhring M, De Carlo S, Crucifix C, Tocchini-Valentini G, Moras D, Schultz P, Poterszman A
EMBO reports
2006-05-01 00:00
7
5
500-5
Department of Structural Biology and Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, rue Laurent Fries, 67404 Illkirch, France.
EMBO Rep.
1469-221X
10.1038/sj.embor.7400663
7400663
0
False
16547462
