In:
PLOS Genetics, Public Library of Science (PLoS), Vol. 18, No. 7 ( 2022-7-11), p. e1010180-
Abstract:
Methionine residues are particularly sensitive to oxidation by reactive oxygen or chlorine species (ROS/RCS), leading to the appearance of methionine sulfoxide in proteins. This post-translational oxidation can be reversed by omnipresent protein repair pathways involving methionine sulfoxide reductases (Msr). In the periplasm of Escherichia coli , the enzymatic system MsrPQ, whose expression is triggered by the RCS, controls the redox status of methionine residues. Here we report that MsrPQ synthesis is also induced by copper stress via the CusSR two-component system, and that MsrPQ plays a role in copper homeostasis by maintaining the activity of the copper efflux pump, CusCFBA. Genetic and biochemical evidence suggest the metallochaperone CusF is the substrate of MsrPQ and our study reveals that CusF methionines are redox sensitive and can be restored by MsrPQ. Thus, the evolution of a CusSR-dependent synthesis of MsrPQ allows conservation of copper homeostasis under aerobic conditions by maintenance of the reduced state of Met residues in copper-trafficking proteins.
Type of Medium:
Online Resource
ISSN:
1553-7404
DOI:
10.1371/journal.pgen.1010180
DOI:
10.1371/journal.pgen.1010180.g001
DOI:
10.1371/journal.pgen.1010180.g002
DOI:
10.1371/journal.pgen.1010180.g003
DOI:
10.1371/journal.pgen.1010180.g004
DOI:
10.1371/journal.pgen.1010180.g005
DOI:
10.1371/journal.pgen.1010180.g006
DOI:
10.1371/journal.pgen.1010180.t001
DOI:
10.1371/journal.pgen.1010180.t002
DOI:
10.1371/journal.pgen.1010180.t003
DOI:
10.1371/journal.pgen.1010180.s001
DOI:
10.1371/journal.pgen.1010180.s002
DOI:
10.1371/journal.pgen.1010180.r001
DOI:
10.1371/journal.pgen.1010180.r002
DOI:
10.1371/journal.pgen.1010180.r003
DOI:
10.1371/journal.pgen.1010180.r004
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2022
detail.hit.zdb_id:
2186725-2
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