Singh, Jayanti ; Anand, Ruchi ; Horovitz, Amnon ; Champion, Patricia A. (2022) Cooperativity in ATP Hydrolysis by MopR Is Modulated by Its Signal Reception Domain and by Its Protein and Phenol Concentrations Journal of Bacteriology, 204 (8). ISSN 0021-9193
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Official URL: http://doi.org/10.1128/jb.00179-22
Related URL: http://dx.doi.org/10.1128/jb.00179-22
Abstract
The NtrC family of AAA+ proteins are bacterial transcriptional regulators that control σ54-dependent RNA polymerase transcription under certain stressful conditions. MopR, which is a member of this family, is responsive to phenol and stimulates its degradation. Biochemical studies to understand the role of ATP and phenol in oligomerization and allosteric regulation, which are described here, show that MopR undergoes concentration-dependent oligomerization in which dimers assemble into functional hexamers. The oligomerization occurs in a nucleation-dependent manner with a tetrameric intermediate. Additionally, phenol binding is shown to be responsible for shifting MopR’s equilibrium from a repressed state (high affinity toward ATP) to a functionally active, derepressed state with low-affinity for ATP. Based on these findings, we propose a model for allosteric regulation of MopR.
Item Type: | Article |
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Source: | Copyright of this article belongs to American Society for Microbiology |
ID Code: | 126667 |
Deposited On: | 28 Sep 2022 04:26 |
Last Modified: | 28 Sep 2022 04:32 |
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