ArticleJournal of experimental botany2017
Co-ordination of NDH and Cup proteins in CO2 uptake in cyanobacterium Synechocystis sp. PCC 6803.
Article in Journal of experimental botany, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 36 citations in OpenAlex.
- Lysine acetylation in cyanobacteria: emerging mechanisms and functions.Biochemical Society transactions · 2025Review
- The regulation of PSI cyclic electron transport by both plastoquinone and ferredoxin redox states: correlation with the rate of proton motive force utilization.Frontiers in plant science · 2025Article
- CupAR negatively controls the key protein CupA in the carbon acquisition complex NDH-1MS in Synechocystis sp. PCC 6803.The Journal of biological chemistry · 2024Article
- Article
- Adapting from Low to High: An Update to COPlants (Basel, Switzerland) · 2023Review
- Cold acclimation alleviates cold stress-induced PSII inhibition and oxidative damage in tobacco leaves.Plant signaling & behavior · 2022Article
- Comparative Genomic Analysis Revealed Distinct Molecular Components and Organization of COFrontiers in microbiology · 2022Article
- Cyanobacterial NDH-1 Complexes.Frontiers in microbiology · 2022Review
- Dissolved Inorganic Carbon-Accumulating Complexes from Autotrophic Bacteria from Extreme Environments.Journal of bacteriology · 2021Article
- Review
- Carbon/nitrogen homeostasis control in cyanobacteria.FEMS microbiology reviews · 2020Review
- Diversity in COApplied and environmental microbiology · 2019Article
- Overcoming adversity through diversity: aquatic carbon concentrating mechanisms.Journal of experimental botany · 2017Article
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4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High and low affinity CO2-uptake systems containing CupA (NDH-1MS) and CupB (NDH-1MS'), respectively, have been identified in Synechocystis sp. PCC 6803, but it is yet unknown how the complexes function in CO2 uptake. In this work, we found that deletion of cupB significantly lowered the growth of cells, and deletion of both cupA and cupB seriously suppressed the growth below pH 7.0 even under 3% CO2. The rate of photosynthetic oxygen evolution was decreased slightly by deletion of cupA but significantly by deletion of cupB and more severely by deletion of both cupA and cupB, especially in response to changed pH conditions under 3% CO2. Furthermore, we found that assembly of CupB into NDH-1MS' was dependent on NdhD4 and NdhF4. NDH-1MS' was not affected in the NDH-1MS-degradation mutant and NDH-1MS was not affected in the NDH-1MS'-degradation mutants, indicating the existence of independent CO2-uptake systems under high CO2 conditions. The light-induced proton gradient across thylakoid membranes was significantly inhibited in ndhD-deletion mutants, suggesting that NdhDs functions in proton pumping. The carbonic anhydrase activity was suppressed partly in the cupA- or cupB-deletion mutant but severely in the mutant with both cupA and cupB deletion, indicating that CupA and CupB function in conversion of CO2 to HCO3-. In turn, deletion of cup genes lowered the transthylakoid membrane proton gradient and deletion of ndhDs decreased the CO2 hydration. Our results suggest that NDH-1M provides an alkaline region to activate Cup proteins involved in CO2 uptake.
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