A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System

IgaA is an integral inner membrane protein that was discovered as repressor of the RcsCDB phosphorelay system in the intracellular pathogen Salmonella enterica serovar Typhimurium. The RcsCDB system, conserved in many members of the family Enterobacteriaceae, regulates expression of varied processes...

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Main Authors: M. Graciela Pucciarelli, Leticia Rodríguez, Francisco García-del Portillo
Format: Article
Language:English
Published: Frontiers Media S.A. 2017-12-01
Series:Frontiers in Microbiology
Subjects:
Online Access:http://journal.frontiersin.org/article/10.3389/fmicb.2017.02605/full
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author M. Graciela Pucciarelli
M. Graciela Pucciarelli
M. Graciela Pucciarelli
Leticia Rodríguez
Francisco García-del Portillo
author_facet M. Graciela Pucciarelli
M. Graciela Pucciarelli
M. Graciela Pucciarelli
Leticia Rodríguez
Francisco García-del Portillo
author_sort M. Graciela Pucciarelli
collection DOAJ
description IgaA is an integral inner membrane protein that was discovered as repressor of the RcsCDB phosphorelay system in the intracellular pathogen Salmonella enterica serovar Typhimurium. The RcsCDB system, conserved in many members of the family Enterobacteriaceae, regulates expression of varied processes including motility, biofilm formation, virulence and response to envelope stress. IgaA is an essential protein to which, in response to envelope perturbation, the outer membrane lipoprotein RcsF has been proposed to bind in order to activate the RcsCDB phosphorelay. Envelope stress has also been reported to be sensed by a surface exposed domain of RcsF. These observations support a tight control of the RcsCDB system by RcsF and IgaA via mechanisms that, however, remain unknown. Interestingly, RcsF and IgaA have four conserved cysteine residues in loops exposed to the periplasmic space. Two non-consecutive disulfide bonds were shown to be required for RcsF function. Here, we report mutagenesis studies supporting the presence of one disulfide bond (C404-C425) in the major periplasmic loop of IgaA that is essential for repression of the RcsCDB phosphorelay. Our data therefore suggest that the redox state of the periplasm may be critical for the control of the RcsCDB system by its two upstream regulators, RcsF and IgaA.
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spelling doaj.art-0a83b6cf642c4f77867ce6f5dbe22b8f2022-12-22T01:53:15ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2017-12-01810.3389/fmicb.2017.02605316123A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB SystemM. Graciela Pucciarelli0M. Graciela Pucciarelli1M. Graciela Pucciarelli2Leticia Rodríguez3Francisco García-del Portillo4Laboratorio de Patógenos Bacterianos Intracelulares, Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, SpainDepartamento de Biología Molecular, Universidad Autónoma de Madrid, Madrid, SpainCentro de Biología Molecular Severo Ochoa-Consejo Superior de Investigaciones Científicas (CBMSO-CSIC), Madrid, SpainLaboratorio de Patógenos Bacterianos Intracelulares, Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, SpainLaboratorio de Patógenos Bacterianos Intracelulares, Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, SpainIgaA is an integral inner membrane protein that was discovered as repressor of the RcsCDB phosphorelay system in the intracellular pathogen Salmonella enterica serovar Typhimurium. The RcsCDB system, conserved in many members of the family Enterobacteriaceae, regulates expression of varied processes including motility, biofilm formation, virulence and response to envelope stress. IgaA is an essential protein to which, in response to envelope perturbation, the outer membrane lipoprotein RcsF has been proposed to bind in order to activate the RcsCDB phosphorelay. Envelope stress has also been reported to be sensed by a surface exposed domain of RcsF. These observations support a tight control of the RcsCDB system by RcsF and IgaA via mechanisms that, however, remain unknown. Interestingly, RcsF and IgaA have four conserved cysteine residues in loops exposed to the periplasmic space. Two non-consecutive disulfide bonds were shown to be required for RcsF function. Here, we report mutagenesis studies supporting the presence of one disulfide bond (C404-C425) in the major periplasmic loop of IgaA that is essential for repression of the RcsCDB phosphorelay. Our data therefore suggest that the redox state of the periplasm may be critical for the control of the RcsCDB system by its two upstream regulators, RcsF and IgaA.http://journal.frontiersin.org/article/10.3389/fmicb.2017.02605/fullSalmonellaIgaAperiplasmic domaincysteinedisulfide bondRcsCDB
spellingShingle M. Graciela Pucciarelli
M. Graciela Pucciarelli
M. Graciela Pucciarelli
Leticia Rodríguez
Francisco García-del Portillo
A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System
Frontiers in Microbiology
Salmonella
IgaA
periplasmic domain
cysteine
disulfide bond
RcsCDB
title A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System
title_full A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System
title_fullStr A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System
title_full_unstemmed A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System
title_short A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System
title_sort disulfide bond in the membrane protein igaa is essential for repression of the rcscdb system
topic Salmonella
IgaA
periplasmic domain
cysteine
disulfide bond
RcsCDB
url http://journal.frontiersin.org/article/10.3389/fmicb.2017.02605/full
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