Structural analysis and dimerization potential of the human TAF5 subunit of TFHD

TFIID is an essential factor required for RNA polymerase II transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2007-01, Vol.104 (4), p.1189
Main Authors: Bhattacharya, Suparna, Takada, Shinako, Jacobson, Raymond H
Format: Article
Language:English
Subjects:
Biochemistry
Proteins
Ribonucleic acid
RNA
RNA polymerase
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:TFIID is an essential factor required for RNA polymerase II transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a structural analysis of the TAF5 protein. Our structure at 2.2-... resolution of the TAF5-NTD2 domain reveals an ...-helical domain with distant structural similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain contains several conserved clefts likely to be critical for TFIID complex assembly. Our biochemical analysis of the human TAF5 protein demonstrates the ability of the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a key property required for the assembly of the TFIID complex. (ProQuest Information and Learning: ... denotes formulae/symbols omitted.)
ISSN:0027-8424
1091-6490