ArticlePlant physiology2016
A Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803.
Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- On the non-oxygenic origins of thylakoids.Communications biology · 2025Review
- A cyanobacteria-derived intermolecular salt bridge stabilizes photosynthetic NDH-1 and prevents oxidative stress.Communications biology · 2025Article
- Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations.Communications biology · 2023Article
- NDH-1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria.Plant direct · 2023Article
- Genetic, Genomics, and Responses to Stresses in Cyanobacteria: Biotechnological Implications.Genes · 2021Review
- PhotoModPlus: A web server for photosynthetic protein prediction from genome neighborhood features.PloS one · 2021Article
- Structural insights into NDH-1 mediated cyclic electron transfer.Nature communications · 2020Article
- NDH-1 Is Important for Photosystem I Function ofFrontiers in plant science · 2017Article
- The NDH-1L-PSI Supercomplex Is Important for Efficient Cyclic Electron Transport in Cyanobacteria.Plant physiology · 2016Article
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6 authors.
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Abstract
Despite significant progress in clarifying the subunit compositions and functions of the multiple NDH-1 complexes in cyanobacteria, the assembly factors and their roles in assembling these NDH-1 complexes remain elusive. Two mutants sensitive to high light for growth and impaired in NDH-1-dependent cyclic electron transport around photosystem I were isolated from Synechocystis sp. strain PCC 6803 transformed with a transposon-tagged library. Both mutants were tagged in the ssl3829 gene encoding an unknown protein, which shares significant similarity with Arabidopsis (Arabidopsis thaliana) CHLORORESPIRATORY REDUCTION7. The ssl3829 product was localized in the cytoplasm and associates with an NDH-1 hydrophilic arm assembly intermediate (NAI) of about 300 kD (NAI300) and an NdhI maturation factor, Slr1097. Upon deletion of Ssl3829, the NAI300 complex was no longer visible on gels, thereby impeding the assembly of the NDH-1 hydrophilic arm. The deletion also abolished Slr1097 and consequently reduced the amount of mature NdhI in the cytoplasm, which repressed the dynamic assembly process of the NDH-1 hydrophilic arm because mature NdhI was essential to stabilize all functional NAIs. Therefore, Ssl3829 plays an important role in the assembly of the NDH-1 hydrophilic arm by accumulating the NAI300 complex and Slr1097 protein in the cytoplasm.
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