ArticleScientific reports2016
NdhV subunit regulates the activity of type-1 NAD(P)H dehydrogenase under high light conditions in cyanobacterium Synechocystis sp. PCC 6803.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 18 citations in OpenAlex.
- Electron transport reactions of cyanobacterial photosynthesis and state-of-the-art in vivo measurement techniques.Plant physiology · 2026Review
- A cyanobacteria-derived intermolecular salt bridge stabilizes photosynthetic NDH-1 and prevents oxidative stress.Communications biology · 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
- Dynamic Changes in the Thylakoid Proteome of Cyanobacteria during Light-Regulated Thylakoid Membrane Development.Plants (Basel, Switzerland) · 2023Article
- Cyanobacterial NDH-1 Complexes.Frontiers in microbiology · 2022Review
- PhotoModPlus: A web server for photosynthetic protein prediction from genome neighborhood features.PloS one · 2021Article
- Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase.Nature communications · 2020Article
- Article
- Analysis of Protein Complexes in the Unicellular Cyanobacterium Cyanothece ATCC 51142.Journal of proteome research · 2018Article
- Co-ordination of NDH and Cup proteins in CO2 uptake in cyanobacterium Synechocystis sp. PCC 6803.Journal of experimental botany · 2017Article
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5 authors at 3 institutions in 1 country.
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Abstract
The cyanobacterial NAD(P)H dehydrogenase (NDH-1) complexes play crucial roles in variety of bioenergetic reactions. However, the regulative mechanism of NDH-1 under stressed conditions is still unclear. In this study, we detected that the NDH-1 activity is partially impaired, but the accumulation of NDH-1 complexes was little affected in the NdhV deleted mutant (ΔndhV) at low light in cyanobacterium Synechocystis sp. PCC 6803. ΔndhV grew normally at low light but slowly at high light under inorganic carbon limitation conditions (low pH or low CO2), meanwhile the activity of CO2 uptake was evidently lowered than wild type even at pH 8.0. The accumulation of NdhV in thylakoids strictly relies on the presence of the hydrophilic subcomplex of NDH-1. Furthermore, NdhV was co-located with hydrophilic subunits of NDH-1 loosely associated with the NDH-1L, NDH-1MS' and NDH-1M complexes. The level of the NdhV was significantly increased at high light and deletion of NdhV suppressed the up-regulation of NDH-1 activity, causing the lowered the photosynthetic oxygen evolution at pH 6.5 and high light. These data indicate that NdhV is an intrinsic subunit of hydrophilic subcomplex of NDH-1, required for efficient operation of cyclic electron transport around photosystem I and CO2 uptake at high lights.
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