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Article Dans Une Revue Journal of Biological Chemistry Année : 2018

The labile interactions of cyclic electron flow effector proteins

Résumé

The supramolecular organization of membrane proteins (MPs) is sensitive to environmental changes in photosynthetic organisms. Isolation of MP supercomplexes from the green algae Chlamydomonas reinhardtii, which are believed to contribute to cyclic electron flow (CEF) between the cytochrome b 6 f complex (Cyt-b 6 f) and photosystem I (PSI), proved difficult. We were unable to isolate a supercomplex containing both Cyt-b 6 f and PSI because in our hands, most of Cyt-b 6 f did not comigrate in sucrose density gradients, even upon using chemical crosslinkers or amphipol substitution of detergents. Assisted by independent affinity purification and MS approaches, we utilized disintegrating MP assemblies and demonstrated that the algaespecific CEF effector proteins PETO and ANR1 are bona fide Cyt-b 6 f interactors, with ANR1 requiring the presence of an additional, presently unknown, protein. We narrowed down the Cyt-b 6 f interface, where PETO is loosely attached to cytochrome f and to a stromal region of subunit IV, which also contains phosphorylation sites for the STT7 kinase.
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Dates et versions

hal-04013242 , version 1 (03-03-2023)

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Felix Buchert, Marion Hamon, Philipp Gäbelein, Martin Scholz, Michael Hippler, et al.. The labile interactions of cyclic electron flow effector proteins. Journal of Biological Chemistry, 2018, 293 (45), pp.17559-17573. ⟨10.1074/jbc.ra118.004475⟩. ⟨hal-04013242⟩
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