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McsB Regulates CtsR Thermosensing Through Peripheral Arginine Phosphorylation.
Huahuan Cai1, Boyang Hua2, Jie Hu3
1Institute of Drug Discovery Technology, Ningbo University, Ningbo 315211, China; Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences, Ningbo University, Ningbo 315211, China.
Journal of Molecular Biology
|September 1, 2025
Summary
Bacterial heat-shock response involves CtsR inactivation by McsB. McsB phosphorylation of CtsR on arginine residues alters its DNA binding, lowering the temperature threshold for dissociation and regulating heat-shock gene expression.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- The bacterial heat-shock response is crucial for survival under elevated temperatures.
- CtsR acts as a master transcription repressor, regulating heat-shock gene expression.
- McsB, an arginine kinase, inactivates CtsR through phosphorylation.
Purpose of the Study:
- To investigate the real-time interactions between DNA, CtsR, and McsB.
- To elucidate the molecular mechanism by which McsB regulates CtsR activity.
- To understand the role of CtsR peripheral arginine residues in thermosensing.
Main Methods:
- Fluorescence Intensity Shift Assay (FISA) using the PIFE effect for real-time monitoring.
- Single-molecule real-time binding assays to determine binding kinetics.
- Mass spectrometry, mutational analysis, and structural simulations.
Main Results:
- CtsR binds rapidly and stably to DNA.
- McsB transiently interacts with DNA-bound CtsR.
- McsB binding lowers the temperature threshold for CtsR dissociation and alters thermosensing.
- Phosphorylation of peripheral arginine residues on CtsR reduces DNA binding energy.
Conclusions:
- McsB regulates CtsR-DNA interactions by modulating CtsR phosphorylation.
- Peripheral arginine residues of CtsR are functionally important in the bacterial heat-shock response.
- This study provides molecular insights into the regulation of bacterial thermosensing.
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