A Nucleus-Encoded Chloroplast Protein YL1 Is Involved in Chloroplast Development and Efficient Biogenesis of Chloroplast ATP Synthase in Rice

• Published in: Scientific reports Vol. 6; no. 1; p. 32295
• Main Authors: Chen, Fei, Dong, Guojun, Wu, Limin, Wang, Fang, Yang, Xingzheng, Ma, Xiaohui, Wang, Haili, Wu, Jiahuan, Zhang, Yanli, Wang, Huizhong, Qian, Qian, Yu, Yanchun
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 02.09.2016; Nature Publishing Group
• Subjects: 14/19; 14/63; 42/70; 45/23; 45/44; 631/449/1659; 631/449/1734; 631/449/2653; 82/1; 82/111; 82/29; ATP; ATP synthase; Biosynthesis; Chlorophyll; Chloroplasts; Complementation; Developmental stages; Evolution; Humanities and Social Sciences; Inactivation; Leaves; multidisciplinary; Nuclei; Oryza sativa; Photochemicals; Photosynthesis; Science; Yeasts; Yellow leaf
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/srep32295

Chloroplast ATP synthase (cpATPase) is an importance thylakoid membrane-associated photosynthetic complex involved in the light-dependent reactions of photosynthesis. In this study, we isolated and characterized a rice ( Oryza sativa ) mutant yellow leaf 1 (yl1 ), which exhibits chlorotic leaves throughout developmental stages. The YL1 mutation showed reduced chlorophyll contents, abnormal chloroplast morphology and decreased photochemical efficiency. Moreover, YL1 deficiency disrupts the expression of genes associated with chloroplast development and photosynthesis. Molecular and genetic analyses revealed that YL1 is a nucleus-encoded protein with a predicted transmembrane domain in its carboxyl-terminus that is conserved in the higher plant kingdom. YL1 localizes to chloroplasts and is preferentially expressed in green tissues containing chloroplasts. Immunoblot analyses showed that inactivation of YL1 leads to drastically reduced accumulation of AtpA (α) and AtpB (β), two core subunits of CF 1 αβ subcomplex of cpATPase, meanwhile, a severe decrease (ca. 41.7%) in cpATPase activity was observed in the yl1-1 mutant compared with the wild type. Furthermore, yeast two-hybrid and bimolecular fluorescence complementation assays revealed a specific interaction between YL1 and AtpB subunit of cpATPase. Taken together, our results suggest that YL1 is a plant lineage-specific auxiliary factor involved in the biogenesis of the cpATPase complex, possibly via interacting with the β-subunit.