作者
Christopher P Selby, Aziz Sancar
发表日期
1997/1/17
期刊
Journal of Biological Chemistry
卷号
272
期号
3
页码范围
1885-1890
出版商
Elsevier
简介
Transcription is coupled to repair in Escherichia coli and in humans. Proteins encoded by the mfd gene in E. coli and by the ERCC6/CSB gene in humans, both of which possess the so-called helicase motifs, are required for the coupling reaction. It has been shown that the Mfd protein is an ATPase but not a helicase and accomplishes coupling, in part, by disrupting the ternary complex of E. coli RNA polymerase stalled at the site of DNA damage. In this study we overproduced the human CSB protein using the baculovirus vector and purified and characterized the recombinant protein. CSB has an ATPase activity that is stimulated strongly by DNA; however, it neither acts as a helicase nor does it dissociate stalled RNA polymerase II, suggesting a coupling mechanism in humans different from that in prokaryotes. CSB is a DNA-binding protein, and it also binds to XPA, TFIIH, and the p34 subunit of TFIIE. These …
引用总数
19971998199920002001200220032004200520062007200820092010201120122013201420152016201720182019202020212022202320241718191416221981313121012857141154988614814