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bioRxiv · 10.1101/2021.10.01.462544

AtCGL160 recruits chloroplast coupling factor 1

Reiter, B.·Rosenhammer, L.·Marino, G.·Geimer, S.·Leister, D.·Rühle, T.
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Abstract

ATP synthases couple the generation of chemical energy to a transmembrane electro-chemical potential. Like ATP synthases in bacteria and mitochondria, chloroplast ATP synthases consist of a membrane-spanning (CFO) and a soluble coupling factor (CF1). Accessory factors facilitate subunit production and orchestrate the assembly of the functional CF1-CFO complex. It was previously shown that the accessory factor 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. In this study, we show that the N-terminal portion of CGL160 (AtCGL160N), which is specific to the green lineage, is required for late steps in CF1-CFO assembly in Arabidopsis thaliana. In plants that lacked this stroma-exposed domain, photosynthesis was impaired, and amounts of CF1-CFO were reduced to about 65% of the wild-type level. Loss of AtCGL160N did not perturb c-ring formation, but led to a 10-fold increase in the numbers of CF1 sub-complexes in the stroma relative to the wild type and the CF1 assembly mutant atcgld11-1. 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 thylakoid-proximal domain of CF1-{beta} that includes the conserved DELSEED motif. We therefore propose that AtCGL160 has acquired an additional function in the recruitment of soluble CF1 to a membrane-integral CFO sub-complex, which is critical for the modulation of CF1-CFO activity and photosynthesis in chloroplasts.

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Reiter, B., Rosenhammer, L., Marino, G., Geimer, S., Leister, D., Rühle, T.. 2021-10-01. AtCGL160 recruits chloroplast coupling factor 1. https://doi.org/10.1101/2021.10.01.462544

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