ArticleThe Plant cell2012
Initial steps of photosystem II de novo assembly and preloading with manganese take place in biogenesis centers in Synechocystis.
Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 100 citations in OpenAlex.
- From proton microdomains to protein migration: hypothesis for ΔpH-controlled PSII relocation.Photosynthesis research · 2026Article
- CurT dosage quantitatively affects thylakoid structure and PSII performance in Synechocystis sp. PCC 6803.The Plant journal : for cell and molecular biology · 2026Article
- Exploring thylakoid emergence: evolution of membrane biogenesis and photosystem II assembly in early-diverging cyanobacteria.The New phytologist · 2026Article
- Exploring Thylakoid Emergence: Evolution of Membrane Biogenesis and Photosystem II assembly in early-diverging Cyanobacteria.bioRxiv : the preprint server for biology · 2026Article
- Ionic regulation of thylakoid membrane architecture: Mg2+-driven destacking and restacking visualized.Plant physiology · 2026Article
- Membranous translation platforms in the chloroplast of Chlamydomonas reinhardtii.Plant physiology · 2025Article
- Study of excess manganese stress response highlights the central role of manganese exporter Mnx for holding manganese homeostasis in the cyanobacteriumMicrobiology (Reading, England) · 2024Article
- The biogenesis and maintenance of PSII: Recent advances and current challenges.The Plant cell · 2024Review
- Structure, biogenesis, and evolution of thylakoid membranes.The Plant cell · 2024Review
- The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis.Nature communications · 2023Article
- Absolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803.Photosynthesis research · 2023Article
- FtsH4 protease controls biogenesis of the PSII complex by dual regulation of high light-inducible proteins.Plant communications · 2023Article
- Proximity Labeling Facilitates Defining the Proteome Neighborhood of Photosystem II Oxygen Evolution Complex in a Model Cyanobacterium.Molecular & cellular proteomics : MCP · 2022Article
- Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification.Photosynthesis research · 2022Article
- Advances in the Understanding of the Lifecycle of Photosystem II.Microorganisms · 2022Review
- Processing of D1 Protein: A Mysterious Process Carried Out in Thylakoid Lumen.International journal of molecular sciences · 2022Review
- Thylakoid attachment to the plasma membrane in Synechocystis sp. PCC 6803 requires the AncM protein.The Plant cell · 2022Article
- Complexome profiling on the Chlamydomonas lpa2 mutant reveals insights into PSII biogenesis and new PSII associated proteins.Journal of experimental botany · 2022Article
- Probing the biogenesis pathway and dynamics of thylakoid membranes.Nature communications · 2021Article
- The availability of neither D2 nor CP43 limits the biogenesis of photosystem II in tobacco.Plant physiology · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the cyanobacterium Synechocystis sp PCC 6803, early steps in thylakoid membrane (TM) biogenesis are considered to take place in specialized membrane fractions resembling an interface between the plasma membrane (PM) and TM. This region (the PratA-defined membrane) is defined by the presence of the photosystem II (PSII) assembly factor PratA (for processing-associated TPR protein) and the precursor of the D1 protein (pD1). Here, we show that PratA is a Mn(2+) binding protein that contains a high affinity Mn(2+) binding site (K(d) = 73 μM) and that PratA is required for efficient delivery of Mn(2+) to PSII in vivo, as Mn(2+) transport is retarded in pratA(-). Furthermore, ultrastructural analyses of pratA(-) depict changes in membrane organization in comparison to the wild type, especially a semicircle-shaped structure, which appears to connect PM and TM, is lacking in pratA(-). Immunogold labeling located PratA and pD1 to these distinct regions at the cell periphery. Thus, PratA is necessary for efficient delivery of Mn(2+) to PSII, leading to Mn(2+) preloading of PSII in the periplasm. We propose an extended model for the spatial organization of Mn(2+) transport to PSII, which is suggested to take place concomitantly with early steps of PSII assembly in biogenesis centers at the cell periphery.
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