A role of the C-terminal part of p44 in the promoter escape activity of transcription factor IIH

The Journal of Biological Chemistry
A Tremeau-BravardJean-Marc Egly

Abstract

The p44 subunit plays a crucial role in the overall activity of the transcription/DNA repair factor TFIIH: on the one hand its N-terminal domain interacts with and regulates the XPD helicase (, ); on the other hand, as shown in the present study, it participates with the promoter escape reaction. Mutagenesis along with recombinant technology using the baculovirus/insect cells expression system allowed us to define the function of the two structural motifs of the C-terminal moiety of p44: mutations within the C4 zinc finger motif (residues 291-308) prevent incorporation of the p62 subunit within the core TFIIH. Double mutations in the RING finger motif (residues 345-385) allow the synthesis of the first phosphodiester bond by RNA polymerase II, but prevent its escape from the promoter. This highlights the role of transcription factor IIH in the various steps of the transcription initiation process.

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Citations

Jan 13, 2005·Environmental and Molecular Mutagenesis·Bernard A KunzEdward J Vonarx
Jan 17, 2004·Biochimie·Renata M A CostaCarlos F M Menck
May 12, 2011·Proceedings of the National Academy of Sciences of the United States of America·Maximiliano M Portal
Feb 7, 2012·Proceedings of the National Academy of Sciences of the United States of America·Brian J GibbonsRoger D Kornberg
Jul 12, 2014·PloS One·Dominik R SchmittCaroline Kisker
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Mar 13, 2019·ELife·Basil J GreberEva Nogales
Jun 25, 2002·The Journal of Biological Chemistry·Anass JawhariJean-Marc Egly
Nov 8, 2007·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Motomi MatsunoYasushi Hiromi
Feb 15, 2015·The Journal of Biological Chemistry·Jin Seok KimYunje Cho

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