Scs system links copper and redox homeostasis in bacterial pathogens

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dc.citation.titleJournal of Biological Chemistry
dc.citation.volume300
dc.creatorMéndez, Andrea A. E.
dc.creatorArgüello, José M.
dc.creatorSoncini, Fernando C.
dc.creatorCheca, Susana Karina
dc.date.accessioned2024-05-02T19:13:19Z
dc.date.available2024-05-02T19:13:19Z
dc.date.issued2021-02-01
dc.description.abstractThe bacterial envelope is an essential compartment involved in metabolism and metabolites transport, virulence, and stress defense. Its roles become more evident when homeostasis is challenged during host–pathogen interactions. In particular, the presence of free radical groups and excess copper in the periplasm causes noxious reactions, such as sulfhydryl group oxidation leading to enzymatic inactivation and protein denaturation. In response to this, canonical and accessory oxidoreductase systems are induced, performing quality control of thiol groups, and therefore contributing to restoring homeostasis and preserving survival under these conditions. Here, we examine recent advances in the characterization of the Dsblike, Salmonella-specific Scs system. This system includes the ScsC/ScsB pair of Cu+-binding proteins with thioloxidoreductase activity, an alternative ScsB-partner, the membrane-linked ScsD, and a likely associated protein, ScsA, with a role in peroxide resistance. We discuss the acquisition of the scsABCD locus and its integration into a global regulatory pathway directing envelope response to Cu stress during the evolution of pathogens that also harbor the canonical Dsb systems. The evidence suggests that the canonical Dsb systems cannot satisfy the extra demands that the host-pathogen interface imposes to preserve functional thiol groups. This resulted in the acquisition of the Scs system by Salmonella. We propose that the ScsABCD complex evolved to connect Cu and redox stress responses in this pathogen as well as in other bacterial pathogens.
dc.description.filFil: Méndez, Andrea A. E. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología Molecular y Celular de Rosario (CONICET-IBR); Argentina.
dc.description.filFil: Argüello, José M. Worcester Polytechnic Institute. Department of Chemistry and Biochemistry; USA.
dc.description.filFil: Soncini, Fernando C. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología Molecular y Celular de Rosario (CONICET-IBR); Argentina.
dc.description.filFil: Checa, Susana Karina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología Molecular y Celular de Rosario (CONICET-IBR); Argentina.
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT): PICT-2018–02122
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Técnicas (CONICET): PIP 11220200100600CO
dc.description.sponsorshipNational Institutes of Health: R01A1150784
dc.format.extent1-10
dc.identifier.issn1083-351X
dc.identifier.urihttps://hdl.handle.net/2133/26975
dc.language.isoen
dc.publisherElsevier
dc.relation.publisherversionhttps://doi.org/10.1016/j.jbc.2024.105710
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S0021925824000863?via%3Dihub
dc.rightsopenAccess
dc.rights.holderMéndez, Andrea A. E.
dc.rights.holderArgüello, José M.
dc.rights.holderSoncini, Fernando C.
dc.rights.holderCheca, Susana Karina
dc.rights.holderUniversidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas
dc.rights.textAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectCu homeostasis
dc.subjectRedox stress
dc.subjectGram-negative bacteria
dc.subjectPeriplasm
dc.subjectThiol oxidoreductase
dc.subjectHost-pathogen interaction
dc.titleScs system links copper and redox homeostasis in bacterial pathogens
dc.typearticulo
dc.type.versionpublishedVersion

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