Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation

Detalhes bibliográficos
Autor(a) principal: Trindade, Inês B.
Data de Publicação: 2023
Outros Autores: Firmino, Maria O., Noordam, Sander J., Alves, Alexandra S., Fonseca, Bruno M., Piccioli, Mario, Louro, Ricardo O.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/158558
Resumo: Funding Information: Financial support was provided by the European EC Horizon2020 TIMB3 (Project 810856) and the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska Curie ITN ConCO2rde (grant agreement No 955740), as well as the COST Action CA21115 Iron–sulphur (FeS) clusters: from chemistry to immunology (FeSImmChemNet). This work was funded by national funds through FC—Fundação para a Ciência e a Tecnologia, I.P. (FCT), Project MOSTMICRO-ITQB with refs UIDB/04612/2020 and UIDP/04612/2020, and the LS4FUTURE Associated Laboratory (LA/P/0087/2020). The N-terminal sequencing service was provided by the ITQB Research facilities. The NMR data were acquired at CERMAX, ITQB-NOVA, Oeiras, Portugal, with equipment funded by the FCT, project AAC 01/SAICT/2016. The IBT was financially supported by national funds through the FCT PT-NMR PhD Program via PD/BD/135187/2017. This work benefited of the support and the use of resources of Instruct-ERIC, specifically the CERM/CIRMMP Italy Centre (PID 4509). Publisher Copyright: © 2023 by the authors.
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spelling Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidationbiological electron transfercytochrome cHIPIPparamagnetic NMRphotoferrotrophismprotein interactionsRhodopseudomonasAnalytical ChemistryChemistry (miscellaneous)Molecular MedicinePharmaceutical ScienceDrug DiscoveryPhysical and Theoretical ChemistryOrganic ChemistryFunding Information: Financial support was provided by the European EC Horizon2020 TIMB3 (Project 810856) and the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska Curie ITN ConCO2rde (grant agreement No 955740), as well as the COST Action CA21115 Iron–sulphur (FeS) clusters: from chemistry to immunology (FeSImmChemNet). This work was funded by national funds through FC—Fundação para a Ciência e a Tecnologia, I.P. (FCT), Project MOSTMICRO-ITQB with refs UIDB/04612/2020 and UIDP/04612/2020, and the LS4FUTURE Associated Laboratory (LA/P/0087/2020). The N-terminal sequencing service was provided by the ITQB Research facilities. The NMR data were acquired at CERMAX, ITQB-NOVA, Oeiras, Portugal, with equipment funded by the FCT, project AAC 01/SAICT/2016. The IBT was financially supported by national funds through the FCT PT-NMR PhD Program via PD/BD/135187/2017. This work benefited of the support and the use of resources of Instruct-ERIC, specifically the CERM/CIRMMP Italy Centre (PID 4509). Publisher Copyright: © 2023 by the authors.Rhodopseudomonas palustris is an alphaproteobacterium with impressive metabolic versatility, capable of oxidizing ferrous iron to fix carbon dioxide using light energy. Photoferrotrophic iron oxidation is one of the most ancient metabolisms, sustained by the pio operon coding for three proteins: PioB and PioA, which form an outer-membrane porin–cytochrome complex that oxidizes iron outside of the cell and transfers the electrons to the periplasmic high potential iron–sulfur protein (HIPIP) PioC, which delivers them to the light-harvesting reaction center (LH-RC). Previous studies have shown that PioA deletion is the most detrimental for iron oxidation, while, the deletion of PioC resulted in only a partial loss. The expression of another periplasmic HiPIP, designated Rpal_4085, is strongly upregulated in photoferrotrophic conditions, making it a strong candidate for a PioC substitute. However, it is unable to reduce the LH-RC. In this work we used NMR spectroscopy to map the interactions between PioC, PioA, and the LH-RC, identifying the key amino acid residues involved. We also observed that PioA directly reduces the LH-RC, and this is the most likely substitute upon PioC deletion. By contrast, Rpal_4085 demontrated significant electronic and structural differences from PioC. These differences likely explain its inability to reduce the LH-RC and highlight its distinct functional role. Overall, this work reveals the functional resilience of the pio operon pathway and further highlights the use of paramagnetic NMR for understanding key biological processes.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNTrindade, Inês B.Firmino, Maria O.Noordam, Sander J.Alves, Alexandra S.Fonseca, Bruno M.Piccioli, MarioLouro, Ricardo O.2023-09-30T22:23:03Z2023-062023-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/158558eng1420-3049PURE: 72787972https://doi.org/10.3390/molecules28124733info: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:RCAAP2024-03-11T05:41:07Zoai:run.unl.pt:10362/158558Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:57:13.088532Repositório 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 Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
title Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
spellingShingle Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
Trindade, Inês B.
biological electron transfer
cytochrome c
HIPIP
paramagnetic NMR
photoferrotrophism
protein interactions
Rhodopseudomonas
Analytical Chemistry
Chemistry (miscellaneous)
Molecular Medicine
Pharmaceutical Science
Drug Discovery
Physical and Theoretical Chemistry
Organic Chemistry
title_short Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
title_full Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
title_fullStr Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
title_full_unstemmed Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
title_sort Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
author Trindade, Inês B.
author_facet Trindade, Inês B.
Firmino, Maria O.
Noordam, Sander J.
Alves, Alexandra S.
Fonseca, Bruno M.
Piccioli, Mario
Louro, Ricardo O.
author_role author
author2 Firmino, Maria O.
Noordam, Sander J.
Alves, Alexandra S.
Fonseca, Bruno M.
Piccioli, Mario
Louro, Ricardo O.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
RUN
dc.contributor.author.fl_str_mv Trindade, Inês B.
Firmino, Maria O.
Noordam, Sander J.
Alves, Alexandra S.
Fonseca, Bruno M.
Piccioli, Mario
Louro, Ricardo O.
dc.subject.por.fl_str_mv biological electron transfer
cytochrome c
HIPIP
paramagnetic NMR
photoferrotrophism
protein interactions
Rhodopseudomonas
Analytical Chemistry
Chemistry (miscellaneous)
Molecular Medicine
Pharmaceutical Science
Drug Discovery
Physical and Theoretical Chemistry
Organic Chemistry
topic biological electron transfer
cytochrome c
HIPIP
paramagnetic NMR
photoferrotrophism
protein interactions
Rhodopseudomonas
Analytical Chemistry
Chemistry (miscellaneous)
Molecular Medicine
Pharmaceutical Science
Drug Discovery
Physical and Theoretical Chemistry
Organic Chemistry
description Funding Information: Financial support was provided by the European EC Horizon2020 TIMB3 (Project 810856) and the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska Curie ITN ConCO2rde (grant agreement No 955740), as well as the COST Action CA21115 Iron–sulphur (FeS) clusters: from chemistry to immunology (FeSImmChemNet). This work was funded by national funds through FC—Fundação para a Ciência e a Tecnologia, I.P. (FCT), Project MOSTMICRO-ITQB with refs UIDB/04612/2020 and UIDP/04612/2020, and the LS4FUTURE Associated Laboratory (LA/P/0087/2020). The N-terminal sequencing service was provided by the ITQB Research facilities. The NMR data were acquired at CERMAX, ITQB-NOVA, Oeiras, Portugal, with equipment funded by the FCT, project AAC 01/SAICT/2016. The IBT was financially supported by national funds through the FCT PT-NMR PhD Program via PD/BD/135187/2017. This work benefited of the support and the use of resources of Instruct-ERIC, specifically the CERM/CIRMMP Italy Centre (PID 4509). Publisher Copyright: © 2023 by the authors.
publishDate 2023
dc.date.none.fl_str_mv 2023-09-30T22:23:03Z
2023-06
2023-06-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/158558
url http://hdl.handle.net/10362/158558
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1420-3049
PURE: 72787972
https://doi.org/10.3390/molecules28124733
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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