Structured and Dynamic Disordered Domains Regulate the Activity of a Multifunctional Anti-σ Factor
Julien Herrou1, Jonathan W Willett1, Sean Crosson2
1Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Mbio
|July 30, 2015
Summary
The anti-σ factor NepR regulates bacterial stress response by controlling partner interactions and enhancing PhyR phosphorylation. Both structured and disordered domains of NepR are crucial for these functions in the general stress response pathway.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- The general stress response (GSR) in alphaproteobacteria is regulated by a multiprotein partner switch involving the anti-σ factor NepR.
- NepR interacts with its cognate ECF σ factor and the anti-anti-σ factor PhyR to control gene transcription under stress conditions.
Purpose of the Study:
- To define the functional roles of structured and intrinsically disordered domains of NepR in partner binding and GSR activation.
- To investigate NepR's influence on PhyR phosphorylation and its implications for GSR regulation.
Main Methods:
- Structural and functional analysis of NepR domains.
- In vitro assays to study NepR-PhyR interactions and PhyR phosphorylation rates.
Main Results:
- Key functional roles for both structured and intrinsically disordered domains of NepR were identified in partner binding and GSR transcription activation.
- NepR was found to significantly stimulate PhyR phosphorylation in vitro, an activity dependent on its structured and disordered domains.
- This highlights a novel role for NepR in directly modulating the activation of its binding partner, PhyR.
Conclusions:
- NepR's structured and intrinsically disordered domains work coordinately to control multiple aspects of the GSR signaling pathway.
- NepR directly influences PhyR phosphorylation, adding a new layer of regulation to the bacterial general stress response.
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