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Dimerization of the Free and Photosystem II-Associated PsbO Protein upon Irradiation with UV Light

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Abstract

The main function of the PsbO protein in photosystem II is to stabilize the water-splitting Mn4CaO5 cluster. The present study shows for the first time that short-term exposure of both isolated and membrane-bound PsbO to UV light led to protein dimerization. A non-covalent dimer of the PsbO protein was detected by gel filtration. Separation of proteins of UV-irradiated PSII membrane fragments by polyacrylamide gel electrophoresis was indicative of the formation of covalent PsbO dimers, as with the isolated PsbO protein. The formation of covalent PsbO dimers following exposure to UV light supports the hypothesis that non-covalent PsbO dimers exist in vivo and may play a regulatory role in PSII.

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Funding

The study was supported as part of State Assignment for the Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences (project no. 122041100274-6).

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Authors and Affiliations

  1. Institute of Fundamental Problems of Biology, Russian Academy of Sciences, 142290, Pushchino, Moscow oblast, Russia

    M. S. Khristin, T. N. Smolova & A. A. Khorobrykh

Authors
  1. M. S. Khristin
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  2. T. N. Smolova
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  3. A. A. Khorobrykh
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Corresponding author

Correspondence to A. A. Khorobrykh.

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Conflict of interests. The authors declare that they have no conflicts of interest.

Statement of the welfare of animals. This article does not contain any studies involving animals or human participants performed by any of the authors.

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Translated by D. Timchenko

Abbreviations: PSII, photosystem II; RC, reaction center; OEC, oxygen-evolving complex; PsbO, manganese-stabilizing protein; PAGE, polyacrylamide gel electrophoresis; DTT, dithiotreitol.

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Khristin, M.S., Smolova, T.N. & Khorobrykh, A.A. Dimerization of the Free and Photosystem II-Associated PsbO Protein upon Irradiation with UV Light. BIOPHYSICS 67, 913–920 (2022). https://doi.org/10.1134/S0006350922060100

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