Structural basis for transcription activation by Crl through tethering of σ and RNA polymerase.

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ID: 47928
2019
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Ranked #82 of 292 articles by views in Proceedings of the National Academy of Sciences of the United States of America

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Abstract
In bacteria, a primary σ-factor associates with the core RNA polymerase (RNAP) to control most transcription initiation, while alternative σ-factors are used to coordinate expression of additional regulons in response to environmental conditions. Many alternative σ-factors are negatively regulated by anti-σ-factors. In , , and many other γ-proteobacteria, the transcription factor Crl positively regulates the alternative σ-regulon by promoting the association of σ with RNAP without interacting with promoter DNA. The molecular mechanism for Crl activity is unknown. Here, we determined a single-particle cryo-electron microscopy structure of Crl-σ-RNAP in an open promoter complex with a σ-regulon promoter. In addition to previously predicted interactions between Crl and domain 2 of σ (σ), the structure, along with -benzoylphenylalanine cross-linking, reveals that Crl interacts with a structural element of the RNAP β'-subunit that we call the β'-clamp-toe (β'CT). Deletion of the β'CT decreases activation by Crl without affecting basal transcription, highlighting the functional importance of the Crl-β'CT interaction. We conclude that Crl activates σ-dependent transcription in part through stabilizing σ-RNAP by tethering σ and the β'CT. We propose that Crl, and other transcription activators that may use similar mechanisms, be designated σ-activators.
Reference Key
cartagena2019structuralproceedings Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Cartagena, Alexis Jaramillo;Banta, Amy B;Sathyan, Nikhil;Ross, Wilma;Gourse, Richard L;Campbell, Elizabeth A;Darst, Seth A;
Journal Proceedings of the National Academy of Sciences of the United States of America
Year 2019
DOI
10.1073/pnas.1910827116
URL
Keywords
crl rna polymerase rpos bacterial stress response cryo-electron microscopy

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