ArticleThe Plant cell2006
LOW PSII ACCUMULATION1 is involved in efficient assembly of photosystem II in Arabidopsis thaliana.
Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 116 papers.
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116 citing papers in PubMed, 243 citations in OpenAlex.
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- Convergent roles of BcGUN4.1, BcSG1, BcCHLH, and BcTPR4 in regulating the leaf greenness of non-heading Chinese cabbage.Molecular horticulture · 2026Article
- The GreenCut protein TEF6 maintains photosystem II homeostasis under high light by stabilizing FtsH accumulation in Chlamydomonas reinhardtii.Plant communications · 2026Article
- Proteome and Phosphoproteome of Tomato Fruit Identify REDUCED CHLOROPLAST COVERAGE 1a as A Ripening Regulator.Genomics, proteomics & bioinformatics · 2025Article
- Assembly-dependent translational feedback regulation of photosynthetic proteins in land plants.Nature plants · 2025Article
- LTD coordinates chlorophyll biosynthesis and LIGHT-HARVESTING CHLOROPHYLL A/B-BINDING PROTEIN transport.The Plant cell · 2025Article
- RESISTANCE TO PHYTOPHTHORA1 promotes cytochrome b559 formation during early photosystem II biogenesis in Arabidopsis.The Plant cell · 2024Article
- Thylakoid protein FPB1 synergistically cooperates with PAM68 to promote CP47 biogenesis and Photosystem II assembly.Nature communications · 2024Article
- Differential heat-response characteristics of two plastid isoforms of triose phosphate isomerase in tomato.Plant biotechnology journal · 2024Article
- Article
- A Ubiquitin-Based Module Directing Protein-Protein Interactions in Chloroplasts.International journal of molecular sciences · 2023Article
- TurboID reveals the proxiomes of Chlamydomonas proteins involved in thylakoid biogenesis and stress response.Plant physiology · 2023Article
- Eukaryote-specific assembly factor DEAP2 mediates an early step of photosystem II assembly in Arabidopsis.Plant physiology · 2023Article
- Supplementing the Nuclear-Encoded PSII Subunit D1 Induces Dramatic Metabolic Reprogramming in Flag Leaves during Grain Filling in Rice.Plants (Basel, Switzerland) · 2023Article
- Tetratricopeptide repeat protein SlREC2 positively regulates cold tolerance in tomato.Plant physiology · 2023Article
- The thylakoid membrane protein NTA1 is an assembly factor of the cytochrome bPlant communications · 2023Article
- Genome-wide association study of drought tolerance traits in sugar beet germplasms at the seedling stage.Frontiers in genetics · 2023Article
- NNature communications · 2022Article
- PALE-GREEN LEAF 1, a rice cpSRP54 protein, is essential for the assembly of the PSI-LHCI supercomplex.Plant direct · 2022Article
- NADP+ supply adjusts the synthesis of photosystem I in Arabidopsis chloroplasts.Plant physiology · 2022Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issuedCORRECTION.2018
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To gain insight into the processes involved in photosystem II (PSII) biogenesis and maintenance, we characterized the low psii accumulation1 (lpa1) mutant of Arabidopsis thaliana, which generally accumulates lower than wild-type levels of the PSII complex. In vivo protein labeling experiments showed that synthesis of the D1 and D2 proteins was greatly reduced in the lpa1 mutant, while other plastid-encoded proteins were translated at rates similar to the wild type. In addition, turnover rates of the PSII core proteins CP47, CP43, D1, and D2 were higher in lpa1 than in wild-type plants. The newly synthesized PSII proteins were assembled into functional protein complexes, but the assembly was less efficient in the mutant. LPA1 encodes a chloroplast protein that contains two tetratricopeptide repeat domains and is an intrinsic membrane protein but not an integral subunit of PSII. Yeast two-hybrid studies revealed that LPA1 interacts with D1 but not with D2, cytochrome b6, or Alb3. Thus, LPA1 appears to be an integral membrane chaperone that is required for efficient PSII assembly, probably through direct interaction with the PSII reaction center protein D1.
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