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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | He, Baoye Chen, Fan Mao, Juan Chi, Wei Ouyang, Min Zhang, Lixin |
| Description | Author Affiliation: Mao J ( Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China); Chi W ( Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China); Ouyang M ( Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China); He B ( Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China); Chen F ( State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100086, China.); Zhang L ( Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China); |
| Abstract | The chloroplast ATP synthase, a multisubunit complex in the thylakoid membrane, catalyzes the light-driven synthesis of ATP, thereby supplying the energy for carbon fixation during photosynthesis. The chloroplast ATP synthase is composed of both nucleus- and chloroplast-encoded proteins that have required the evolution of novel mechanisms to coordinate the biosynthesis and assembly of chloroplast ATP synthase subunits temporally and spatially. Here we have elucidated the assembly mechanism of the $α_{3}β_{3}γ$ core complex of the chloroplast ATP synthase by identification and functional characterization of a key assembly factor, PAB (PROTEIN IN CHLOROPLAST ATPASE BIOGENESIS). PAB directly interacts with the nucleus-encoded γ subunit and functions downstream of chaperonin 60 (Cpn60)-mediated $CF_{1}γ$ subunit folding to promote its assembly into the catalytic core. PAB does not have any recognizable motifs or domains but is conserved in photosynthetic eukaryotes. It is likely that PAB evolved together with the transfer of chloroplast genes into the nucleus to assist nucleus-encoded $CF_{1}γ$ assembly into the $CF_{1}$ core. Such coordination might represent an evolutionarily conserved mechanism for folding and assembly of nucleus-encoded proteins to ensure proper assembly of multiprotein photosynthetic complexes. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 13 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Arabidopsis Proteins Metabolism Arabidopsis Chaperonin 60 Chloroplast Proton-Translocating ATPases Chloroplasts Molecular Chaperones Adenosine Triphosphate Catalysis Catalytic Domain Genetics Endopeptidase K Chemistry Green Fluorescent Proteins Phenotype Photosynthesis Protein Folding Thylakoids Two-Hybrid System Techniques Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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