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Structural basis of bacterial transcription activation.
- Source :
-
Science (New York, N.Y.) [Science] 2017 Nov 17; Vol. 358 (6365), pp. 947-951. - Publication Year :
- 2017
-
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 σ <superscript>70</superscript> -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.<br /> (Copyright © 2017, American Association for the Advancement of Science.)
- Subjects :
- Cryoelectron Microscopy
Cyclic AMP Receptor Protein ultrastructure
DNA, Bacterial chemistry
DNA, Bacterial ultrastructure
DNA-Directed RNA Polymerases ultrastructure
Escherichia coli Proteins ultrastructure
Promoter Regions, Genetic
Sigma Factor ultrastructure
Cyclic AMP Receptor Protein chemistry
DNA-Directed RNA Polymerases chemistry
Escherichia coli genetics
Escherichia coli Proteins chemistry
Gene Expression Regulation, Bacterial
Sigma Factor chemistry
Transcriptional Activation
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 358
- Issue :
- 6365
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 29146813
- Full Text :
- https://doi.org/10.1126/science.aao1923