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The two alternative NADH: quinone oxidoreductases from Staphylococcus aureus

2024-08Artigo científico Acesso aberto
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dc.contributor.authorSena, Filipa V.
dc.contributor.authorSousa, Filipe M.
dc.contributor.authorPereira, Ana R.
dc.contributor.authorCatarino, Teresa
dc.contributor.authorCabrita, Eurico J.
dc.contributor.authorPinho, Mariana G.
dc.contributor.authorPinto, Francisco R.
dc.contributor.authorPereira, Manuela M.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.pblAmerican Society for Microbiology
dc.date.accessioned2024-10-29T00:33:41Z
dc.date.available2024-10-29T00:33:41Z
dc.date.issued2024-08
dc.descriptionFunding Information: F.V.S. and F.M.S. were recipients of fellowships by Fundação para a Ciência e a Tecnologia within the scope of the PhD program Molecular Biosciences PD/00133/2012. Publisher Copyright: © 2024 Sena et al.
dc.description.abstractStaphylococcus aureus is an opportunistic pathogen that has emerged as a major public health threat due to the increased incidence of its drug resistance. S. aureus presents a remarkable capacity to adapt to differentniches due to the plasticity of its energy metabolism. In this work, we investigated the energy metabolism of S. aureus, focusing on the alternative NADH:quinone oxidoreductases, NDH-2s. S. aureus presents two genes encoding NDH-2s (NDH-2A and NDH-2B) and lacks genes coding for Complex I, the canonical respiratory NADH:quinone oxidoreductase. This observation makes the action of NDH-2s crucial for the regeneration of NAD+ and, consequently, for the progression of metabolism. Our study involved the comprehensive biochemical characterization of NDH-2B and the exploration of the cellular roles of NDH-2A and NDH-2B, utilizing knockout mutants (Δndh-2a and Δndh-2b). We show that NDH-2B uses NADPH instead of NADH, does not establish a charge-transfer complex in the presence of NADPH, and its reduction by this substrate is the catalytic rate-limiting step. In the case of NDH-2B, the reduction of the flavinis inherently slow, and we suggest the establishment of a charge transfer complex between NADP+ and FADH2, as previously observed for NDH-2A, to slow down quinone reduction and, consequently, prevent the overproduction of reactive oxygen species, which is potentially unnecessary. Furthermore, we observed that the lack of NDH-2A or NDH-2B impacts cell growth, volume, and division differently.The absence of these enzymes results in distinct metabolic phenotypes, emphasizing the unique cellular roles of each NDH-2 in energy metabolism.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent24
dc.format.extent2998004
dc.identifier.doi10.1128/spectrum.04152-23
dc.identifier.issn2165-0497
dc.identifier.otherPURE: 99131336
dc.identifier.otherPURE UUID: 062ed43f-df89-482b-ab51-de6c7bf9a88d
dc.identifier.otherScopus: 85201029856
dc.identifier.otherWOS: 001268104800001
dc.identifier.otherPubMed: 39012110
dc.identifier.otherPubMedCentral: PMC11302666
dc.identifier.urihttp://hdl.handle.net/10362/174200
dc.identifier.urlhttps://www.scopus.com/pages/publications/85201029856
dc.language.isoeng
dc.peerreviewedyes
dc.relationinfo:eu-repo/grantAgreement/FCT//PD%2FBD%2F113985%2F2015/PT
dc.relationinfo:eu-repo/grantAgreement/FCT//PD%2FBD%2F128213%2F2016/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-BQM%2F2599%2F2021/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04046%2F2020/PT
dc.relationBiosystems and Integrative Sciences Institute
dc.subjectalternative NADH oxidase
dc.subjectcharge-transfer complex
dc.subjectmembrane proteins
dc.subjectmonotopic proteins
dc.subjectNAD(P)H
dc.subjectquinones
dc.subjectrespiratory chain
dc.subjectPhysiology
dc.subjectEcology
dc.subjectGeneral Immunology and Microbiology
dc.subjectGenetics
dc.subjectMicrobiology (medical)
dc.subjectCell Biology
dc.subjectInfectious Diseases
dc.subjectSDG 3 - Good Health and Well-being
dc.titleThe two alternative NADH: quinone oxidoreductases from Staphylococcus aureusen
dc.title.subtitletwo players with differentmolecular and cellular rolesen
dc.typejournal article
degois.publication.issue8
degois.publication.titleMicrobiology Spectrum
degois.publication.volume12
dspace.entity.typePublication
oaire.awardNumberPD/BD/113985/2015
oaire.awardNumberPD/BD/128213/2016
oaire.awardNumberPTDC/BIA-BQM/2599/2021
oaire.awardNumberUIDB/04046/2020
oaire.awardNumberUIDP/04046/2020
oaire.awardTitleBiosystems and Integrative Sciences Institute
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//PD%2FBD%2F113985%2F2015/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//PD%2FBD%2F128213%2F2016/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-BQM%2F2599%2F2021/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04046%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/Concurso de avaliação no âmbito do Programa Plurianual de Financiamento de Unidades de I&D (2017%2F2018) - Financiamento Programático/UIDP%2F04046%2F2020/PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStreamConcurso de avaliação no âmbito do Programa Plurianual de Financiamento de Unidades de I&D (2017/2018) - Financiamento Programático
project.funder.identifierhttp://doi.org/10.13039/501100001871
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project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
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