ArticlePlant physiology2015
Subunit Q Is Required to Stabilize the Large Complex of NADPH Dehydrogenase in Synechocystis sp. Strain PCC 6803.
Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- A cyanobacteria-derived intermolecular salt bridge stabilizes photosynthetic NDH-1 and prevents oxidative stress.Communications biology · 2025Article
- Genome-wide insights into the evolutionary history of conserved photosynthetic NDH-1 in cyanobacteria.Frontiers in plant science · 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
- Screening of mutants using chlorophyll fluorescence.Journal of plant research · 2021Article
- Genetic, Genomics, and Responses to Stresses in Cyanobacteria: Biotechnological Implications.Genes · 2021Review
- Transcriptomic responses of Microcystis aeruginosa under electromagnetic radiation exposure.Scientific reports · 2021Article
- The Significance of Chloroplast NAD(P)H Dehydrogenase Complex and Its Dependent Cyclic Electron Transport in Photosynthesis.Frontiers in plant science · 2021Review
- NaGenomics, proteomics & bioinformatics · 2020Article
- Molecular dynamics and structural models of the cyanobacterial NDH-1 complex.Biochimica et biophysica acta. Bioenergetics · 2019Article
- 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
- NdhV subunit regulates the activity of type-1 NAD(P)H dehydrogenase under high light conditions in cyanobacterium Synechocystis sp. PCC 6803.Scientific reports · 2016Article
- Functional Characterization of the Subunits N, H, J, and O of the NAD(P)H Dehydrogenase Complexes in Synechocystis sp. Strain PCC 6803.Plant physiology · 2016Article
- A Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803.Plant physiology · 2016Article
- NdhV Is a Subunit of NADPH Dehydrogenase Essential for Cyclic Electron Transport in Synechocystis sp. Strain PCC 6803.Plant physiology · 2016Article
- Article
- Oscillation Kinetics of Post-illumination Increase in Chl Fluorescence in Cyanobacterium Synechocystis PCC 6803.Frontiers in plant science · 2016Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two major complexes of NADPH dehydrogenase (NDH-1) have been identified in cyanobacteria. A large complex (NDH-1L) contains NdhD1, NdhF1, and NdhP, which are absent in a medium size complex (NDH-1M). They play important roles in respiration, NDH-1-dependent cyclic electron transport around photosystem I, and CO2 uptake. Two mutants sensitive to high light for growth and impaired in cyclic electron transport around photosystem I were isolated from the cyanobacterium Synechocystis sp. strain PCC 6803 transformed with a transposon-bearing library. Both mutants had a tag in an open reading frame encoding a product highly homologous to NdhQ, a single-transmembrane small subunit of the NDH-1L complex, identified in Thermosynechococcus elongatus by proteomics strategy. Deletion of ndhQ disassembled about one-half of the NDH-1L to NDH-1M and consequently impaired respiration, but not CO2 uptake. During prolonged incubation of the thylakoid membrane with n-dodecyl-β-D-maltoside at room temperature, the rest of the NDH-1L in ΔndhQ was disassembled completely to NDH-1M and was much faster than in the wild type. In the ndhP-deletion mutant (ΔndhP) background, absence of NdhQ almost completely disassembled the NDH-1L to NDH-1M, similar to the results observed in the ΔndhD1/ΔndhD2 mutant. We therefore conclude that both NdhQ and NdhP are essential to stabilize the NDH-1L complex.
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