Tfb6, a previously unidentified subunit of the general transcription factor TFIIH, facilitates dissociation of Ssl2 helicase after transcription initiation

被引:21
|
作者
Murakami, Kenji [1 ]
Gibbons, Brian J. [1 ]
Davis, Ralph E. [1 ]
Nagai, Shigeki [1 ]
Liu, Xin [1 ]
Robinson, Philip J. J. [1 ]
Wu, Tinghe [1 ]
Kaplan, Craig D. [2 ]
Kornberg, Roger D. [1 ]
机构
[1] Stanford Univ, Dept Biol Struct, Stanford, CA 94305 USA
[2] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
关键词
DNA repair; general transcription factor; RNA polymerase II; TFIIK; transcription pre-initiation complex; yeast; RNA-POLYMERASE-II; DNA-REPAIR; MESSENGER-RNA; COMPONENT; COMPLEX; KINASE;
D O I
10.1073/pnas.1201448109
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
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页码:4816 / 4821
页数:6
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