CGL160-mediated recruitment of the coupling factor CF1 is required for efficient thylakoid ATP synthase assembly, photosynthesis, and chloroplast development in Arabidopsis.

Autor:	Reiter B; Plant Molecular Biology Faculty of Biology I, Ludwig-Maximilians-Universität Munich, D-82152 Planegg-Martinsried, Germany., Rosenhammer L; Plant Molecular Biology Faculty of Biology I, Ludwig-Maximilians-Universität Munich, D-82152 Planegg-Martinsried, Germany., Marino G; Plant Molecular Biology Faculty of Biology I, Ludwig-Maximilians-Universität Munich, D-82152 Planegg-Martinsried, Germany., Geimer S; Zellbiologie/Elektronenmikroskopie NW I/B1, Universität Bayreuth, 95447 Bayreuth, Germany., Leister D; Plant Molecular Biology Faculty of Biology I, Ludwig-Maximilians-Universität Munich, D-82152 Planegg-Martinsried, Germany., Rühle T; Plant Molecular Biology Faculty of Biology I, Ludwig-Maximilians-Universität Munich, D-82152 Planegg-Martinsried, Germany.
Jazyk:	angličtina
Zdroj:	The Plant cell [Plant Cell] 2023 Jan 02; Vol. 35 (1), pp. 488-509.
DOI:	10.1093/plcell/koac306
Abstrakt:	Chloroplast ATP synthases consist of a membrane-spanning coupling factor (CFO) and a soluble coupling factor (CF1). It was previously demonstrated that CONSERVED ONLY IN THE GREEN LINEAGE160 (CGL160) promotes the formation of plant CFO and performs a similar function in the assembly of its c-ring to that of the distantly related bacterial Atp1/UncI protein. Here, we show that in Arabidopsis (Arabidopsis thaliana) the N-terminal portion of CGL160 (AtCGL160N) is required for late steps in CF1-CFO assembly. In plants that lacked AtCGL160N, CF1-CFO content, photosynthesis, and chloroplast development were impaired. Loss of AtCGL160N did not perturb c-ring formation, but led to a 10-fold increase in the numbers of stromal CF1 subcomplexes relative to that in the wild type. Co-immunoprecipitation and protein crosslinking assays revealed an association of AtCGL160 with CF1 subunits. Yeast two-hybrid assays localized the interaction to a stretch of AtCGL160N that binds to the DELSEED-containing CF1-β subdomain. Since Atp1 of Synechocystis (Synechocystis sp. PCC 6803) could functionally replace the membrane domain of AtCGL160 in Arabidopsis, we propose that CGL160 evolved from a cyanobacterial ancestor and acquired an additional function in the recruitment of a soluble CF1 subcomplex, which is critical for the modulation of CF1-CFO activity and photosynthesis. (© The Author(s) 2022. Published by Oxford University Press on behalf of American Society of Plant Biologists.)
Databáze:	MEDLINE
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