Thylakoid protein FPB1 synergistically cooperates with PAM68 to promote CP47 biogenesis and Photosystem II assembly

Lin Zhang, Junxiang Ruan, Fudan Gao, Qiang Xin, Li-Ping Che, Lujuan Cai, Zekun Liu, Mengmeng Kong, Jean-David Rochaix, Hualing Mi and Lianwei Peng ()
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Lin Zhang: Shanghai Normal University
Junxiang Ruan: Shanghai Normal University
Fudan Gao: Shanghai Normal University
Qiang Xin: Shanghai Normal University
Li-Ping Che: Shanghai Normal University
Lujuan Cai: Shanghai Normal University
Zekun Liu: Shanghai Normal University
Mengmeng Kong: Chinese Academy of Science
Jean-David Rochaix: University of Geneva
Hualing Mi: Chinese Academy of Science
Lianwei Peng: Shanghai Normal University

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract In chloroplasts, insertion of proteins with multiple transmembrane domains (TMDs) into thylakoid membranes usually occurs in a co-translational manner. Here, we have characterized a thylakoid protein designated FPB1 (Facilitator of PsbB biogenesis1) which together with a previously reported factor PAM68 (Photosynthesis Affected Mutant68) is involved in assisting the biogenesis of CP47, a subunit of the Photosystem II (PSII) core. Analysis by ribosome profiling reveals increased ribosome stalling when the last TMD segment of CP47 emerges from the ribosomal tunnel in fpb1 and pam68. FPB1 interacts with PAM68 and both proteins coimmunoprecipitate with SecY/E and Alb3 as well as with some ribosomal components. Thus, our data indicate that, in coordination with the SecY/E translocon and the Alb3 integrase, FPB1 synergistically cooperates with PAM68 to facilitate the co-translational integration of the last two CP47 TMDs and the large loop between them into thylakoids and the PSII core complex.

Date: 2024
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DOI: 10.1038/s41467-024-46863-y

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