p52 mediates XPB function within the transcription/repair factor TFIIH
p52 mediates XPB function within the transcription/repair factor TFIIH
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DOI：
10.1074/jbc.m203792200
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发表时间：
2002-08-30
影响因子：
4.8
通讯作者：
Egly, JM
中科院分区：
文献类型：
--
作者：
Jawhari, A;Lainé, JP;Egly, JM
为了进一步了解转录/DNA修复因子TFIIH，我们研究了其p52亚基在TFIIH功能中的作用。使用一个完全重建的体外转录或核苷酸切除修复（NER）系统，我们表明，删除的G末端区域的p52的结果在TFIIH NER和转录活性的显着减少。该突变阻止启动子打开，并且对TFIIH的其他酶活性没有影响。此外，我们证明，需要完整的p52锚的XPB解旋酶内TFIIH，提供了一个解释的转录和NER缺陷观察到的突变p52。我们表明，这两个亚基物理相互作用和地图领域参与的接口。综上所述，我们的结果表明，TFIIH的p52/Tfb 2亚基通过如先前针对p44和XPD所述的成对相互作用来调节XPB的功能。
To further our understanding of the transcription/DNA repair factor TFIIH, we investigated the role of its p52 subunit in TFIIH function. Using a completely reconstituted in vitro transcription or nucleotide excision repair (NER) system, we show that deletion of the G terminal region of p52 results in a dramatic reduction of TFIIH NER and transcription activities. This mutation prevents promoter opening and has no effect on the other enzymatic activities of TFIIH. Moreover, we demonstrate that intact p52 is needed to anchor the XPB helicase within TFIIH, providing an explanation for the transcription and NER defects observed with the mutant p52. We show that these two subunits physically interact and map domains involved in the interface. Taken together, our results show that the p52/Tfb2 subunit of TFIIH regulates the function of XPB through pair-wise interactions as described previously for p44 and XPD.