The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH.

ABSTRACT: The general transcription factor IIH (TFIIH) is a multi-protein complex and its 10 subunits are engaged in an intricate protein-protein interaction network critical for the regulation of its transcription and DNA repair activities that are so far little understood on a molecular level. In this study, we focused on the p44 and the p34 subunits, which are central for the structural integrity of core-TFIIH. We solved crystal structures of a complex formed by the p34 N-terminal vWA and p44 C-terminal zinc binding domains from Chaetomium thermophilum and from Homo sapiens. Intriguingly, our functional analyses clearly revealed the presence of a second interface located in the C-terminal zinc binding region of p34, which can rescue a disrupted interaction between the p34 vWA and the p44 RING dom

SUBMITTER: Radu L 

PROVIDER: S-EPMC5737387 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature