Structural basis of bacterial transcription activation

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Science  17 Nov 2017:
Vol. 358, Issue 6365, pp. 947-951
DOI: 10.1126/science.aao1923

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Structural basis for transcription activation

Bacteria can initiate transcription through two independent classes of recruitment mechanisms. Liu et al. determined the cryo-electron microscopy structure of an intact class I transcription activation complex. The positions and orientations of all the components and the detailed protein-protein and protein-nucleic acid interactions reveal how an activator interacts with the promoter DNA and recruits RNA polymerase through the class I mechanism. Together with a recently reported class II transcription activation complex, the findings complete our structural understanding of bacterial transcription activation.

Science, this issue p. 947


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 σ70–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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