期刊
CELL
卷 124, 期 3, 页码 507-520出版社
CELL PRESS
DOI: 10.1016/j.cell.2005.11.045
关键词
-
资金
- Biotechnology and Biological Sciences Research Council [BB/C507053/1] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/C507053/1] Funding Source: Medline
- NIGMS NIH HHS [GM44025, GM073829] Funding Source: Medline
Coupling of transcription and DNA repair in bacteria is mediated by transcription-repair coupling factor (TRCF, the product of the mfd gene), which removes transcription elongation complexes stalled at DNA lesions and recruits the nucleotide excision repair machinery to the site. Here we describe the 3.2 angstrom-resolution X-ray crystal structure of Escherichia coli TRCF. The structure consists of a compact arrangement of eight domains, including a translocation module similar to the SF2 ATPase RecG, and a region of structural similarity to UvrB. Biochemical and genetic experiments establish that another domain with structural similarity to the Tudor-like domain of the transcription elongation factor NusG plays a critical role in TRCF/RNA polymerase interactions. Comparison with the translocation module of RecG as well as other structural features indicate that TRCF function involves largescale conformational changes. These data, along with a structural model for the interaction of TRCF with the transcription elongation complex, provide mechanistic insights into TRCF function.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据