PAB is an assembly chaperone that functions downstream of chaperonin 60 in the assembly of chloroplast ATP synthase coupling factor 1

Proceedings of the National Academy of Sciences of the United States of America
Juan MaoLixin Zhang

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 α3β3γ 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 CF1γ 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 CF1γ assembly into the CF1 core. Such coordination might represent an evolutionarily conserved mechanism for folding and assembly of nucleus-encoded proteins to e...Continue Reading

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Citations

Jul 26, 2016·Frontiers in Plant Science·Madlles Q MartinsJosé C Ramalho
Feb 7, 2018·Frontiers in Molecular Biosciences·Qian Zhao, Cuimin Liu
Jan 21, 2017·F1000Research·Ulf-Ingo FlüggeDario Leister
Oct 9, 2015·The Journal of Biological Chemistry·Joshua K EndowKentaro Inoue
Aug 21, 2020·Proceedings of the National Academy of Sciences of the United States of America·Prakitchai Chotewutmontri, Alice Barkan
Nov 17, 2020·Frontiers in Plant Science·Zhikun DuanLianwei Peng

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