Structural analysis and dimerization potential of the human TAF5 subunit of TFIID.

ABSTRACT: 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-A resolution of the TAF5-NTD2 domain reveals an alpha-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.

SUBMITTER: Bhattacharya S 

PROVIDER: S-EPMC1783120 | biostudies-literature | 2007 Jan

REPOSITORIES: biostudies-literature