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Structure and oligomeric state of human transcription factor TFIIE
Author(s) -
Jawhari Anass,
Uhring Muriel,
De Carlo Sacha,
Crucifix Corinne,
TocchiniValentini Guiseppe,
Moras Dino,
Schultz Patrick,
Poterszman Arnaud
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400663
Subject(s) - transcription factor ii e , transcription preinitiation complex , rna polymerase ii , transcription factor ii a , transcription factor ii f , general transcription factor , biology , microbiology and biotechnology , rna polymerase ii holoenzyme , transcription factor , biophysics , chemistry , promoter , biochemistry , gene expression , transcriptional regulation , gene
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 α/β heterodimers as well as a small proportion of tetramers. Analytical ultracentrifugation, chemical crosslinking, pulldown experiments and cryo‐electron microscopy confirmed that TFIIE is a α/β heterodimer in solution. Three‐dimensional envelopes of the α/β 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.