Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Evidence for the I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength

Stepan D. Osipov
,
Yury L. Ryzhykau
ORCID logo ,
Egor V. Zinovev
,
Andronika V. Minaeva
ORCID logo ,
Sergey D. Ivashchenko
,
Dmitry P. Verteletskiy
,
Vsevolod V. Sudarev
,
Daria D. Kuklina
ORCID logo ,
Mikhail Yu. Nikolaev
,
Yury S. Semenov
,
Yuliya A. Zagryadskaya
,
Ivan S. Okhrimenko
,
Margarita S. Gette
,
Alexander I. Kuklin
,
Valentin Ivanovich
,
Vladimir N. Uversky
* ORCID logo ,
Alexey V. Vlasov
*
Version 1 : Received: 2 May 2023 / Approved: 4 May 2023 / Online: 4 May 2023 (03:21:52 CEST)

A peer-reviewed article of this Preprint also exists.

Osipov, S.D.; Ryzhykau, Y.L.; Zinovev, E.V.; Minaeva, A.V.; Ivashchenko, S.D.; Verteletskiy, D.P.; Sudarev, V.V.; Kuklina, D.D.; Nikolaev, M.Y.; Semenov, Y.S.; et al. I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength. Int. J. Mol. Sci. 2023, 24, 10720. https://doi.org/10.3390/ijms241310720 Osipov, S.D.; Ryzhykau, Y.L.; Zinovev, E.V.; Minaeva, A.V.; Ivashchenko, S.D.; Verteletskiy, D.P.; Sudarev, V.V.; Kuklina, D.D.; Nikolaev, M.Y.; Semenov, Y.S.; et al. I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength. Int. J. Mol. Sci. 2023, 24, 10720. https://doi.org/10.3390/ijms241310720

Abstract

F-type ATP synthases play a key role in oxidative and photophosphorylation processes producing adenosine triphosphate (ATP) for most biochemical reactions in living organisms. In contrast to the mitochondrial FOF1-ATP synthases those of chloroplasts are known to be mostly monomers with approx. 15% fraction of oligomers interacting presumably non-specifically in a thylakoid membrane. To shed light to the nature of this difference we studied interactions of the chloroplast ATP synthases using small-angle X-ray scattering (SAXS) method. Here, we report evidence of I-shaped dimerization of solubilized FOF1-ATP synthases from spinach chloroplasts at different salinity. The structural data were obtained by SAXS and showed dimerization in response to changes in ionic strength. The best model describing SAXS data was two ATP-synthases connected through F1/F1’ parts, presumably via their δ-subunits, forming dimers with the “I” shape. Such I-shaped dimers might possibly connect the neighboring lamellae in thylakoid stacks assuming that the FOF1 monomers comprising such dimers are embedded in different thylakoid membranes. If this type of dimerization exists in nature, it might be one of the pathways of inhibition of chloroplast FOF1-ATP synthase for preventing of ATP hydrolysis in dark, when salinity in plant chloroplasts is rising. Together with a redox switch inserted into a γ-subunit of chloroplast FOF1 and lateral oligomerization, an I-shaped dimerization might comprise a subtle regulatory process of ATP synthesis and stabilize the structure of thylakoid stacks in chloroplasts.

Keywords

FOF1-ATP synthase; chloroplasts; dimers; small-angle scattering; membrane proteins

Subject

Biology and Life Sciences, Biophysics

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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