Tfb6, a previously unidentified subunit of the general transcription factor TFIIH, facilitates dissociation of Ssl2 helicase after transcription initiation.
Abstract
General transcription factor TFIIH, previously described as a 10-subunit complex, is essential for transcription and DNA repair. An eleventh subunit now identified, termed Tfb6, exhibits 45% sequence similarity to human nuclear mRNA export factor 5. Tfb6 dissociates from TFIIH as a heterodimer with the Ssl2 subunit, a DNA helicase that drives promoter melting for the initiation of transcription. Tfb6 does not, however, dissociate Ssl2 from TFIIH in the context of a fully assembled transcription preinitiation complex. Our findings suggest a dynamic state of Ssl2, allowing its engagement in multiple cellular processes.
Links
Authors
Murakami K, Gibbons BJ, Davis RE, Nagai S, Liu X, Robinson PJ, Wu T, Kaplan CD, Kornberg RD
Institution
Department of Structural Biology, Stanford University, Stanford, CA 94305, USA.
Source
Proceedings of the National Academy of Sciences of the United States of America 109:13 2012 Mar 27 pg 4816-21MeSH
Chromatography, LiquidDNA Helicases
Gene Deletion
Gene Expression Regulation, Fungal
Humans
Mass Spectrometry
Phenotype
Phosphorylation
Protein Binding
Protein Subunits
RNA, Messenger
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Temperature
Transcription Factor TFIIH
Transcription Factors
Transcription, Genetic
Ultraviolet Rays
Pub Type(s)
Journal ArticleResearch Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Language
eng
PubMed ID
22411836
Log In

