ArticleNature communications2024
Thylakoid protein FPB1 synergistically cooperates with PAM68 to promote CP47 biogenesis and Photosystem II assembly.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The AtRNC1-AtWTF1 protein complex is essential for chloroplast group Ⅱ intron splicing, ribosome biogenesis, and embryo development in Arabidopsis.Plant molecular biology · 2026Article
- The lumenal domain of Cyt bPhotosynthesis research · 2025Article
- Complexome profiling of the Chlamydomonas psb28 mutant reveals TEF5 as an early PSII assembly factor.The Plant cell · 2025Article
- Thylakoids for enhanced photodynamic therapy in hypoxic tumours.Science and technology of advanced materials · 2025Review
- Transcriptome time-course analysis unravels the regulatory networks governing ratooning decline in sugarcane.Frontiers in plant science · 2025Article
- Localization of proteins involved in the biogenesis and repair of the photosynthetic apparatus to thylakoid subdomains inPlant direct · 2024Article
- RESISTANCE TO PHYTOPHTHORA1 promotes cytochrome b559 formation during early photosystem II biogenesis in Arabidopsis.The Plant cell · 2024Article
- A cargo sorting receptor mediates chloroplast protein trafficking through the secretory pathway.The Plant cell · 2024Article
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Authors and funding
11 authors.
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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.
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