期刊
SCIENCE
卷 349, 期 6250, 页码 882-885出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aab1478
关键词
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资金
- Chinese National Science Foundation
- China Scholarship Council
- UK Biotechnology and Biological Sciences Research Council
- NIH [GM087350, R37 GM37048]
- National Key Basic Research Programme in China [2015CB755700]
- BBSRC [BB/J00717X/1, BB/L027135/1] Funding Source: UKRI
- MRC [MR/N006828/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L027135/1, BB/C504700/1, BB/J00717X/1, 1377217] Funding Source: researchfish
- Medical Research Council [MR/N006828/1] Funding Source: researchfish
- Wellcome Trust [098412/Z/12/Z] Funding Source: researchfish
Transcription by RNA polymerase (RNAP) in bacteria requires specific promoter recognition by sigma factors. The major variant s factor (sigma(54)) initially forms a transcriptionally silent complex requiring specialized adenosine triphosphate-dependent activators for initiation. Our crystal structure of the 450-kilodalton RNAP-sigma(54) holoenzyme at 3.8 angstroms reveals molecular details of sigma(54) and its interactions with RNAP. The structure explains how sigma(54) targets different regions in RNAP to exert its inhibitory function. Although sigma(54) and the major s factor, sigma(70), have similar functional domains and contact similar regions of RNAP, unanticipated differences are observed in their domain arrangement and interactions with RNAP, explaining their distinct properties. Furthermore, we observe evolutionarily conserved regulatory hotspots in RNAPs that can be targeted by a diverse range of mechanisms to fine tune transcription.
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