Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility

Detalhes bibliográficos
Autor(a) principal: Trindade, Inês B.
Data de Publicação: 2019
Outros Autores: Silva, José M., Fonseca, Bruno M., Catarino, Teresa, Fujita, Masaki, Matias, Pedro M., Moe, Elin, Louro, Ricardo O.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://doi.org/10.1074/jbc.RA118.005041
Resumo: This work was supported by the European Union’s Horizon 2020 research and innovation program under Grant 810856, National Funds Grant ERA-MBT/ 0003/2014, Ph.D. fellowship PD/BD/135187/2017 (to I. B. T.), and postdoctoral fellowships SFRH/BPD/94050/2013 and SFRH/BPD/93164/2013 (to E. M. and B. F. M.), through the FCT-Fundação para a Ciência e Tecnologia. The authors declare that they have no conflicts of interest with the contents of this article. Acknowledgments—We thank Isabel Pacheco for help in the purification of SfSIP and Dr. Américo Duarte for providing ferredoxin. We also thank all members of the Inorganic Biochemistry and NMR Laboratory for discussions and comments and feedback regarding the preparation of the manuscript. The NMR experiments were performed at CERMAX (Centro de Ressonância Magnetica António Xavier) and was financially supported by Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular) funded by FEDER funds through COMPETE2020-Programa Opera-cional Competitividade e Internacionalização (POCI), the European Community’s Seventh Framework Program (FP7/2007–2013)) under Grant Agreement 283570 (BioStruct-X). Beamtime at I04 at the Diamond Light Source and assistance from the beamline staff during the synchrotron data collections are gratefully acknowledged.
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spelling Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatilityBiochemistryMolecular BiologyCell BiologySDG 14 - Life Below WaterThis work was supported by the European Union’s Horizon 2020 research and innovation program under Grant 810856, National Funds Grant ERA-MBT/ 0003/2014, Ph.D. fellowship PD/BD/135187/2017 (to I. B. T.), and postdoctoral fellowships SFRH/BPD/94050/2013 and SFRH/BPD/93164/2013 (to E. M. and B. F. M.), through the FCT-Fundação para a Ciência e Tecnologia. The authors declare that they have no conflicts of interest with the contents of this article. Acknowledgments—We thank Isabel Pacheco for help in the purification of SfSIP and Dr. Américo Duarte for providing ferredoxin. We also thank all members of the Inorganic Biochemistry and NMR Laboratory for discussions and comments and feedback regarding the preparation of the manuscript. The NMR experiments were performed at CERMAX (Centro de Ressonância Magnetica António Xavier) and was financially supported by Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular) funded by FEDER funds through COMPETE2020-Programa Opera-cional Competitividade e Internacionalização (POCI), the European Community’s Seventh Framework Program (FP7/2007–2013)) under Grant Agreement 283570 (BioStruct-X). Beamtime at I04 at the Diamond Light Source and assistance from the beamline staff during the synchrotron data collections are gratefully acknowledged.Siderophores make iron accessible under iron-limited conditions and play a crucial role in the survival of microorganisms. Because of their remarkable metal-scavenging properties and ease in crossing cellular envelopes, siderophores hold great potential in biotechnological applications, raising the need for a deeper knowledge of the molecular mechanisms underpinning the siderophore pathway. Here, we report the structural and functional characterization of a siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIBM400 (SfSIP). SfSIP is a flavin-containing ferric-siderophore reductase with FAD- and NAD(P)H-binding domains that have high homology with other characterized SIPs. However, we found here that it mechanistically departs from what has been described for this family of proteins. Unlike other FAD-containing SIPs, SfSIP did not discriminate between NADH and NADPH. Furthermore, SfSIP required the presence of the Fe 2+ -scavenger, ferrozine, to use NAD(P)H to drive the reduction of Shewanella-produced hydroxamate ferric-siderophores. Additionally, this is the first SIP reported that also uses a ferredoxin as electron donor, and in contrast to NAD(P)H, its utilization did not require the mediation of ferrozine, and electron transfer occurred at fast rates. Finally, FAD oxidation was thermodynamically coupled to deprotonation at physiological pH values, enhancing the solubility of ferrous iron. On the basis of these results and the location of the SfSIP gene downstream of a sequence for putative binding of aerobic respiration control protein A (ArcA), we propose that SfSIP contributes an additional layer of regulation that maintains cellular iron homeostasis according to environmental cues of oxygen availability and cellular iron demand.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)DQ - Departamento de QuímicaRUNTrindade, Inês B.Silva, José M.Fonseca, Bruno M.Catarino, TeresaFujita, MasakiMatias, Pedro M.Moe, ElinLouro, Ricardo O.2023-02-08T01:31:50Z2019-01-012019-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article11application/pdfhttps://doi.org/10.1074/jbc.RA118.005041eng0021-9258PURE: 11734449http://www.scopus.com/inward/record.url?scp=85059495865&partnerID=8YFLogxKhttps://doi.org/10.1074/jbc.RA118.005041info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:30:04Zoai:run.unl.pt:10362/63431Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:33:55.398104Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility
title Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility
spellingShingle Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility
Trindade, Inês B.
Biochemistry
Molecular Biology
Cell Biology
SDG 14 - Life Below Water
title_short Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility
title_full Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility
title_fullStr Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility
title_full_unstemmed Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility
title_sort Structure and reactivity of a siderophore-interacting protein from the marine bacterium Shewanella reveals unanticipated functional versatility
author Trindade, Inês B.
author_facet Trindade, Inês B.
Silva, José M.
Fonseca, Bruno M.
Catarino, Teresa
Fujita, Masaki
Matias, Pedro M.
Moe, Elin
Louro, Ricardo O.
author_role author
author2 Silva, José M.
Fonseca, Bruno M.
Catarino, Teresa
Fujita, Masaki
Matias, Pedro M.
Moe, Elin
Louro, Ricardo O.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Trindade, Inês B.
Silva, José M.
Fonseca, Bruno M.
Catarino, Teresa
Fujita, Masaki
Matias, Pedro M.
Moe, Elin
Louro, Ricardo O.
dc.subject.por.fl_str_mv Biochemistry
Molecular Biology
Cell Biology
SDG 14 - Life Below Water
topic Biochemistry
Molecular Biology
Cell Biology
SDG 14 - Life Below Water
description This work was supported by the European Union’s Horizon 2020 research and innovation program under Grant 810856, National Funds Grant ERA-MBT/ 0003/2014, Ph.D. fellowship PD/BD/135187/2017 (to I. B. T.), and postdoctoral fellowships SFRH/BPD/94050/2013 and SFRH/BPD/93164/2013 (to E. M. and B. F. M.), through the FCT-Fundação para a Ciência e Tecnologia. The authors declare that they have no conflicts of interest with the contents of this article. Acknowledgments—We thank Isabel Pacheco for help in the purification of SfSIP and Dr. Américo Duarte for providing ferredoxin. We also thank all members of the Inorganic Biochemistry and NMR Laboratory for discussions and comments and feedback regarding the preparation of the manuscript. The NMR experiments were performed at CERMAX (Centro de Ressonância Magnetica António Xavier) and was financially supported by Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular) funded by FEDER funds through COMPETE2020-Programa Opera-cional Competitividade e Internacionalização (POCI), the European Community’s Seventh Framework Program (FP7/2007–2013)) under Grant Agreement 283570 (BioStruct-X). Beamtime at I04 at the Diamond Light Source and assistance from the beamline staff during the synchrotron data collections are gratefully acknowledged.
publishDate 2019
dc.date.none.fl_str_mv 2019-01-01
2019-01-01T00:00:00Z
2023-02-08T01:31:50Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.uri.fl_str_mv https://doi.org/10.1074/jbc.RA118.005041
url https://doi.org/10.1074/jbc.RA118.005041
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0021-9258
PURE: 11734449
http://www.scopus.com/inward/record.url?scp=85059495865&partnerID=8YFLogxK
https://doi.org/10.1074/jbc.RA118.005041
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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