期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 114, 期 10, 页码 E1805-E1814出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1619464114
关键词
RNA polymerase; sigma 54; sigma N; transcription; X-ray crystallography
资金
- National Institute of General Medical Sciences from the NIH [P41 GM103403]
- Argonne National Laboratory [DE-AC02-06CH11357]
- DOE Office of Basic Energy Sciences
- Center for Synchrotron Biosciences from the National Institute of Biomedical Imaging and Bioengineering
- Women in Science Fellowship at The Rockefeller University
- NIH [R35 GM118130]
The bacterial sigma factors confer promoter specificity to the RNA polymerase (RNAP). One alternative sigma factor, sigma(N), is unique in its structure and functional mechanism, forming transcriptionally inactive promoter complexes that require activation by specialized AAA(+) ATPases. We report a 3.4- angstrom resolution X-ray crystal structure of a sigma(N) fragment in complex with its cognate promoter DNA, revealing the molecular details of promoter recognition by sigma(N). The structure allowed us to build and refine an improved sigma(N)-holoenzyme model based on previously published 3.8-angstrom resolution X-ray data. The improved sigma(N)-holoenzyme model reveals a conserved interdomain interface within sigma(N) that, when disrupted by mutations, leads to transcription activity without activator intervention (so-called bypass mutants). Thus, the structure and stability of this interdomain interface are crucial for the role of sigma(N) in blocking transcription activity and in maintaining the activator sensitivity of sigma(N).
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