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

Lauri Nikkanen, Anita Santana Sánchez, Maria Ermakova, Matthias Rögner, Laurent Cournac, Yagut Allahverdiyeva*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    36 Citations (Scopus)

    Abstract

    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 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.

    Original languageEnglish
    Pages (from-to)1460-1476
    Number of pages17
    JournalPlant Journal
    Volume103
    Issue number4
    DOIs
    Publication statusPublished - 1 Aug 2020

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