Roles of methionine and cysteine residues of the Escherichia coli sensor kinase HprS in reactive chlorine species sensing

Author:

Yamaji Kotaro12,Taniguchi Rumine12,Urano Hiroyuki12,Ogasawara Hiroshi12345ORCID

Affiliation:

1. Division of Gene Research, Research Center for Advanced Science and Technology Shinshu University Ueda Japan

2. Department of Applied Biology, Graduate School of Science and Technology Shinshu University Ueda Japan

3. Academic Assembly School of Humanities and Social Sciences Institute of Humanities Shinshu University Matsumoto Japan

4. Renaissance Center for Applied Microbiology Nagano Japan

5. Institute for Fiber Engineering (IFES), Interdisciplinary Cluster for Cutting Edge Research (ICCER) Shinshu University Nagano Japan

Abstract

Sensor histidine kinase HprS, an oxidative stress sensor of Escherichia coli, senses reactive oxygen species (ROS) and reactive chlorine species (RCS), and is involved in the induction of oxidatively damaged protein repair periplasmic enzymes. We reinvestigated the roles of six methionine and four cysteine residues of HprS in the response to HClO, an RCS. The results of site‐directed mutagenesis revealed that methionine residues in periplasmic and cytoplasmic regions (Met225) are involved in HprS activation. Interestingly, the Cys165Ser substitution reduced HprS activity, which was recovered by an additional Glu22Cys substitution. Our results demonstrate that the position of the inner membrane cysteine residues influences the extent of HprS activation in HClO sensing.

Funder

Ministry of Education, Culture, Sports, Science and Technology

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

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