ArticlePlant physiology2013
The gene sml0013 of Synechocystis species strain PCC 6803 encodes for a novel subunit of the NAD(P)H oxidoreductase or complex I that is ubiquitously distributed among Cyanobacteria.
Article in Plant physiology, 2013. 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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18 citing papers in PubMed, 32 citations in OpenAlex.
- A cyanobacteria-derived intermolecular salt bridge stabilizes photosynthetic NDH-1 and prevents oxidative stress.Communications biology · 2025Article
- Analysis of a photosynthetic cyanobacterium rich in internal membrane systems via gradient profiling by sequencing (Grad-seq).The Plant cell · 2021Article
- Phycobilisome breakdown effector NblD is required to maintain the cellular amino acid composition during nitrogen starvation.Journal of bacteriology · 2021Article
- AcnSP - A Novel Small Protein Regulator of Aconitase Activity in the CyanobacteriumFrontiers in microbiology · 2020Article
- Heterocyst Thylakoid Bioenergetics.Life (Basel, Switzerland) · 2019Review
- Analysis of Protein Complexes in the Unicellular Cyanobacterium Cyanothece ATCC 51142.Journal of proteome research · 2018Article
- PProceedings of the National Academy of Sciences of the United States of America · 2018Article
- 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
- NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO2 Uptake in Synechocystis sp. Strain PCC 6803.The Journal of biological chemistry · 2016Article
- Oscillation Kinetics of Post-illumination Increase in Chl Fluorescence in Cyanobacterium Synechocystis PCC 6803.Frontiers in plant science · 2016Article
- NDH-1L interacts with ferredoxin via the subunit NdhS in Thermosynechococcus elongatus.Photosynthesis research · 2015Article
- Regulatory RNAs in photosynthetic cyanobacteria.FEMS microbiology reviews · 2015Review
- Regulation of CO2 Concentrating Mechanism in Cyanobacteria.Life (Basel, Switzerland) · 2015Review
- NdhO, a subunit of NADPH dehydrogenase, destabilizes medium size complex of the enzyme in Synechocystis sp. strain PCC 6803.The Journal of biological chemistry · 2014Article
- NdhP is an exclusive subunit of large complex of NADPH dehydrogenase essential to stabilize the complex in Synechocystis sp. strain PCC 6803.The Journal of biological chemistry · 2014Article
- The 5 kDa protein NdhP is essential for stable NDH-1L assembly in Thermosynechococcus elongatus.PloS one · 2014Article
- Electron transport and light-harvesting switches in cyanobacteria.Frontiers in plant science · 2014Review
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5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NAD(P)H oxidoreductase or complex I (NDH1) complex participates in many processes such as respiration, cyclic electron flow, and inorganic carbon concentration in the cyanobacterial cell. Despite immense progress in our understanding of the structure-function relation of the cyanobacterial NDH1 complex, the subunits catalyzing NAD(P)H docking and oxidation are still missing. The gene sml0013 of Synechocystis 6803 encodes for a small protein of unknown function for which homologs exist in all completely known cyanobacterial genomes. The protein exhibits weak similarities to the NDH-dependent flow6 (NDF6) protein, which was reported from Arabidopsis (Arabidopsis thaliana) chloroplasts as a NDH subunit. An sml0013 inactivation mutant of Synechocystis 6803 was generated and characterized. It showed only weak differences regarding growth and pigmentation in various culture conditions; most remarkably, it exhibited a glucose-sensitive phenotype in the light. The genome-wide expression pattern of the Δsml0013::Km mutant was almost identical to the wild type when grown under high CO2 conditions as well as after shifts to low CO2 conditions. However, measurements of the photosystem I redox kinetic in cells of the Δsml0013::Km mutant revealed differences, such as a decreased capability of cyclic electron flow as well as electron flow into respiration in comparison with the wild type. These results suggest that the Sml0013 protein (named NdhP) represents a novel subunit of the cyanobacterial NDH1 complex, mediating its coupling either to the respiratory or the photosynthetic electron flow.
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