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Functional redundancy between flavodiiron proteins and NDH-1 in Synechocystis sp. PCC 6803

Nikkanen, Lauri; Sanchez, Anita Santana; Ermakova, Maria; Rogner, Matthias; Cournac, Laurent; Allahverdiyeva, Yagut

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In oxygenic photosynthetic organisms, excluding angiosperms, flavodiiron proteins (FDPs) catalyze light‐dependent reduction of O2 to H2O. This alleviates electron pressure on the photosynthetic apparatus and protects it from photodamage. In Synechocystis sp. PCC 6803, four FDP isoforms function as hetero‐oligomers of Flv1 and Flv3 and/or Flv2 and Flv4. An alternative electron transport pathway mediated by the NAD(P)H dehydrogenase‐like complex (NDH‐1) also contributes to redox hemostasis and...[Show more]

dc.contributor.authorNikkanen, Lauri
dc.contributor.authorSanchez, Anita Santana
dc.contributor.authorErmakova, Maria
dc.contributor.authorRogner, Matthias
dc.contributor.authorCournac, Laurent
dc.contributor.authorAllahverdiyeva, Yagut
dc.date.accessioned2021-02-22T23:41:49Z
dc.date.available2021-02-22T23:41:49Z
dc.identifier.issn0960-7412
dc.identifier.urihttp://hdl.handle.net/1885/224135
dc.description.abstractIn oxygenic photosynthetic organisms, excluding angiosperms, flavodiiron proteins (FDPs) catalyze light‐dependent reduction of O2 to H2O. This alleviates electron pressure on the photosynthetic apparatus and protects it from photodamage. In Synechocystis sp. PCC 6803, four FDP isoforms function as hetero‐oligomers of Flv1 and Flv3 and/or Flv2 and Flv4. An alternative electron transport pathway mediated by the NAD(P)H dehydrogenase‐like complex (NDH‐1) also contributes to redox hemostasis and the photoprotection of photosynthesis. Four NDH‐1 types have been characterized in cyanobacteria: NDH‐11 and NDH‐12, which function in respiration; and NDH‐13 and NDH‐14, which function in CO2 uptake. All four types are involved in cyclic electron transport. Along with single FDP mutants (∆flv1 and Δflv3) and the double NDH‐1 mutants (∆d1d2, which is deficient in NDH‐11,2 and ∆d3d4, which is deficient in NDH‐13,4), we studied triple mutants lacking one of Flv1 or Flv3, and NDH‐11,2 or NDH‐13,4. We show that the presence of either Flv1/3 or NDH‐11,2, but not NDH‐13,4, is indispensable for survival during changes in growth conditions from high CO2/moderate light to low CO2/high light. Our results show functional redundancy between FDPs and NDH‐11,2 under the studied conditions. We suggest that ferredoxin probably functions as a primary electron donor to both Flv1/3 and NDH‐11,2, allowing their functions to be dynamically coordinated for efficient oxidation of photosystem I and for photoprotection under variable CO2 and light availability
dc.description.sponsorshipThis work was supported by the Academy of Finland (project no. 315119 to Y.A. and the Finnish Center of Excellence, project no. 307335), the NordForsk Nordic Center of Excellence ‘NordAqua’ (no. 82845) and SFB480, Germany.
dc.format.mimetypeapplication/pdf
dc.language.isoen_AU
dc.publisherBlackwell Publishing Ltd
dc.rights© 2020 The Authors
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceThe Plant Journal
dc.subjectFlavodiiron proteins
dc.subjectFlv
dc.subjectNDH-1
dc.subjectphotosynthesis
dc.subjectSynechocystis sp. PCC 6803
dc.subjectcyanobacteria
dc.subjectMehler-like reaction
dc.subjectalternative electron transfer
dc.subjectphotoprotection.
dc.titleFunctional redundancy between flavodiiron proteins and NDH-1 in Synechocystis sp. PCC 6803
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume103
dcterms.dateAccepted2020-05-05
dc.date.issued2020-05-11
local.identifier.absfor060114 - Systems Biology
local.identifier.ariespublicationa383154xPUB13403
local.publisher.urlhttps://onlinelibrary.wiley.com/
local.type.statusPublished Version
local.contributor.affiliationNikkanen, Lauri, University of Turku
local.contributor.affiliationSanchez, Anita Santana, University of Turku
local.contributor.affiliationErmakova, Maria, College of Science, ANU
local.contributor.affiliationRogner, Matthias, Ruhr University Bochum
local.contributor.affiliationCournac, Laurent, University of Montpellier
local.contributor.affiliationAllahverdiyeva, Yagut, University of Turku
local.bibliographicCitation.issue4
local.bibliographicCitation.startpage1460
local.bibliographicCitation.lastpage1476
local.identifier.doi10.1111/tpj.14812
local.identifier.absseo970106 - Expanding Knowledge in the Biological Sciences
dc.date.updated2020-11-15T07:18:22Z
dcterms.accessRightsOpen Access
dc.provenanceThis is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
dc.rights.licenseCreative Commons Attribution License
CollectionsANU Research Publications

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