A kinase-deficient transcription factor TFIIH is functional in basal and activated transcription

Tomi P. Mäkelä, Jeffrey D. Parvin, Jaesang Kim, L. Julie Huber, Phillip A. Sharp, Robert A. Weinberg

Research output: Contribution to journalArticlepeer-review

111 Scopus citations

Abstract

Phosphorylation of the carboxyl-terminal domain (CTD) of the large subunit of RNA polymerase II has been suggested to be critical for transcription initiation, activation, or elongation. A kinase activity specific for CTD is a component of the general transcription factor TFIIH. Recently, a cyclin- dependent kinase-activator kinase (MO15 and cyclin H) was found to be associated with TFIIH preparations and was suggested to be the CTD kinase, TFIIH preparations containing mutant, kinase-deficient MO15 lack CTD kinase activity, indicating that MO15 is critical for polymerase phosphorylation. Nonetheless, these mutant TFIIH preparations were fully functional (in vitro) in both basal and activated transcription. These results indicate that CTD phosphorylation is not required for transcription with a highly purified system.

Original languageEnglish
Pages (from-to)5174-5178
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number11
DOIs
StatePublished - 23 May 1995

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