期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 13, 页码 9126-9134出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.430900
关键词
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资金
- National Institutes of Health Grant [GM087350-A1]
- Center of Excellence of the Japan Society for the Promotion of Science
- Human Frontier Science Program
Escherichia coli RNA polymerase (RNAP) is the most studied bacterial RNAP and has been used as the model RNAP for screening and evaluating potential RNAP-targeting antibiotics. However, the x-ray crystal structure of E. coli RNAP has been limited to individual domains. Here, I report the x-ray structure of the E. coli RNAP sigma(70) holoenzyme, which shows sigma region 1.1 (sigma(1.1)) and the alpha subunit C-terminal domain for the first time in the context of an intact RNAP. sigma(1.1) is positioned at the RNAP DNA-binding channel and completely blocks DNA entry to the RNAP active site. The structure reveals that sigma(1.1) contains a basic patch on its surface, which may play an important role in DNA interaction to facilitate open promoter complex formation. The alpha subunit C-terminal domain is positioned next to sigma domain 4 with a fully stretched linker between the N- and C-terminal domains. E. coli RNAP crystals can be prepared from a convenient overexpression system, allowing further structural studies of bacterial RNAP mutants, including functionally deficient and antibiotic-resistant RNAPs.
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