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Article: Regulation of DNA-binding activity of the Staphylococcus aureus catabolite control protein A by copper (II)-mediated oxidation

TitleRegulation of DNA-binding activity of the Staphylococcus aureus catabolite control protein A by copper (II)-mediated oxidation
Authors
Issue Date2022
Citation
Journal of Biological Chemistry, 2022, v. 298, n. 3, article no. 101587 How to Cite?
AbstractCatabolite control protein A (CcpA) of the human pathogen Staphylococcus aureus is an essential DNA regulator for carbon catabolite repression and virulence, which facilitates bacterial survival and adaptation to a changing environment. Here, we report that copper (II) signaling mediates the DNA-binding capability of CcpA in vitro and in vivo. Copper (II) catalyzes the oxidation of two cysteine residues (Cys216 and Cys242) in CcpA to form intermolecular disulfide bonds between two CcpA dimers, which results in the formation and dissociation of a CcpA tetramer of CcpA from its cognate DNA promoter. We further demonstrate that the two cysteine residues on CcpA are important for S. aureus to resist host innate immunity, indicating that S. aureus CcpA senses the redox-active copper (II) ions as a natural signal to cope with environmental stress. Together, these findings reveal a novel regulatory mechanism for CcpA activity through copper (II)-mediated oxidation.
Persistent Identifierhttp://hdl.handle.net/10722/313037
ISSN
2020 Impact Factor: 5.157
2023 SCImago Journal Rankings: 1.766
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLiao, Xiangwen-
dc.contributor.authorLi, Huinan-
dc.contributor.authorGuo, Yu-
dc.contributor.authorYang, Fang-
dc.contributor.authorChen, Yushou-
dc.contributor.authorHe, Xiaojun-
dc.contributor.authorLi, Hongyan-
dc.contributor.authorXia, Wei-
dc.contributor.authorMao, Zong Wan-
dc.contributor.authorSun, Hongzhe-
dc.date.accessioned2022-05-26T07:00:09Z-
dc.date.available2022-05-26T07:00:09Z-
dc.date.issued2022-
dc.identifier.citationJournal of Biological Chemistry, 2022, v. 298, n. 3, article no. 101587-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/313037-
dc.description.abstractCatabolite control protein A (CcpA) of the human pathogen Staphylococcus aureus is an essential DNA regulator for carbon catabolite repression and virulence, which facilitates bacterial survival and adaptation to a changing environment. Here, we report that copper (II) signaling mediates the DNA-binding capability of CcpA in vitro and in vivo. Copper (II) catalyzes the oxidation of two cysteine residues (Cys216 and Cys242) in CcpA to form intermolecular disulfide bonds between two CcpA dimers, which results in the formation and dissociation of a CcpA tetramer of CcpA from its cognate DNA promoter. We further demonstrate that the two cysteine residues on CcpA are important for S. aureus to resist host innate immunity, indicating that S. aureus CcpA senses the redox-active copper (II) ions as a natural signal to cope with environmental stress. Together, these findings reveal a novel regulatory mechanism for CcpA activity through copper (II)-mediated oxidation.-
dc.languageeng-
dc.relation.ispartofJournal of Biological Chemistry-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleRegulation of DNA-binding activity of the Staphylococcus aureus catabolite control protein A by copper (II)-mediated oxidation-
dc.typeArticle-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1016/j.jbc.2022.101587-
dc.identifier.pmid35032550-
dc.identifier.pmcidPMC8847796-
dc.identifier.scopuseid_2-s2.0-85125012832-
dc.identifier.volume298-
dc.identifier.issue3-
dc.identifier.spagearticle no. 101587-
dc.identifier.epagearticle no. 101587-
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000791267400011-

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