期刊
SCIENCE
卷 358, 期 6365, 页码 947-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aao1923
关键词
-
资金
- NIH [GM22778]
In bacteria, the activation of gene transcription at many promoters is simple and only involves a single activator. The cyclic adenosine 3', 5'-monophosphate receptor protein (CAP), a classic activator, is able to activate transcription independently through two different mechanisms. Understanding the class I mechanism requires an intact transcription activation complex (TAC) structure at a high resolution. Here we report a high-resolution cryo-electron microscopy structure of an intact Escherichia coli class I TAC containing a CAP dimer, a sigma(70) -RNA polymerase (RNAP) holoenzyme, a complete class I CAP-dependent promoter DNA, and a de novo synthesized RNA oligonucleotide. The structure shows how CAP wraps the upstream DNA and how the interactions recruit RNAP. Our study provides a structural basis for understanding how activators activate transcription through the class I recruitment mechanism.
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