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Science. 2017 Nov 17;358(6365):947-951. doi: 10.1126/science.aao1923.

Structural basis of bacterial transcription activation.

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
2
Howard Hughes Medical Institute, CryoEM Shared Resource, Janelia Research Campus, Ashburn, VA 20147, USA.
3
Howard Hughes Medical Institute, CryoEM Shared Resource, Janelia Research Campus, Ashburn, VA 20147, USA. thomas.steitz@yale.edu yuz@janelia.hhmi.org.
4
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. thomas.steitz@yale.edu yuz@janelia.hhmi.org.
5
Howard Hughes Medical Institute, Yale University, New Haven, CT 06510, USA.
6
Department of Chemistry, Yale University, New Haven, CT 06520, USA.

Abstract

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.

PMID:
29146813
DOI:
10.1126/science.aao1923
[Indexed for MEDLINE]

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