Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 13, Pages 9126-9134Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.430900
Keywords
-
Categories
Funding
- National Institutes of Health Grant [GM087350-A1]
- Center of Excellence of the Japan Society for the Promotion of Science
- Human Frontier Science Program
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available