ArticlePloS one2014
The 5 kDa protein NdhP is essential for stable NDH-1L assembly in Thermosynechococcus elongatus.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Unveiling a novel broad-host-range cyanomyovirus cross-infecting Prochlorococcus and Synechococcus.BMC biology · 2025Article
- Dynamic Changes in the Thylakoid Proteome of Cyanobacteria during Light-Regulated Thylakoid Membrane Development.Plants (Basel, Switzerland) · 2023Article
- NDH-1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria.Plant direct · 2023Article
- The Significance of Chloroplast NAD(P)H Dehydrogenase Complex and Its Dependent Cyclic Electron Transport in Photosynthesis.Frontiers in plant science · 2021Review
- Redox-coupled proton pumping drives carbon concentration in the photosynthetic complex I.Nature communications · 2020Article
- AcnSP - A Novel Small Protein Regulator of Aconitase Activity in the CyanobacteriumFrontiers in microbiology · 2020Article
- Molecular dynamics and structural models of the cyanobacterial NDH-1 complex.Biochimica et biophysica acta. Bioenergetics · 2019Article
- Article
- Metabolic engineering of Synechococcus elongatus PCC 7942 for improvement of 1,3-propanediol and glycerol production based on in silico simulation of metabolic flux distribution.Microbial cell factories · 2017Article
- Co-ordination of NDH and Cup proteins in CO2 uptake in cyanobacterium Synechocystis sp. PCC 6803.Journal of experimental botany · 2017Article
- Transmission Electron Microscopy as a Tool for the Characterization of Soft Materials: Application and Interpretation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2017Review
- A Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803.Plant physiology · 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
- NdhV Is a Subunit of NADPH Dehydrogenase Essential for Cyclic Electron Transport in Synechocystis sp. Strain PCC 6803.Plant physiology · 2016Article
- Recent advances in understanding photosynthesis.F1000Research · 2016Review
- NDH-1L interacts with ferredoxin via the subunit NdhS in Thermosynechococcus elongatus.Photosynthesis research · 2015Article
- Proteomic approaches in research of cyanobacterial photosynthesis.Photosynthesis research · 2015Review
- Subunit Q Is Required to Stabilize the Large Complex of NADPH Dehydrogenase in Synechocystis sp. Strain PCC 6803.Plant physiology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cyanobacterial NADPH:plastoquinone oxidoreductase complex (NDH-1), that is related to Complex I of eubacteria and mitochondria, plays a pivotal role in respiration as well as in cyclic electron transfer (CET) around PSI and is involved in a unique carbon concentration mechanism (CCM). Despite many achievements in the past, the complex protein composition and the specific function of many subunits of the different NDH-1 species remain elusive. We have recently discovered in a NDH-1 preparation from Thermosynechococcus elongatus two novel single transmembrane peptides (NdhP, NdhQ) with molecular weights below 5 kDa. Here we show that NdhP is a unique component of the ∼ 450 kDa NDH-1L complex, that is involved in respiration and CET at high CO2 concentration, and not detectable in the NDH-1MS and NDH-1MS' complexes that play a role in carbon concentration. C-terminal fusion of NdhP with his-tagged superfolder GFP and the subsequent analysis of the purified complex by electron microscopy and single particle averaging revealed its localization in the NDH-1L specific distal unit of the NDH-1 complex, that is formed by the subunits NdhD1 and NdhF1. Moreover, NdhP is essential for NDH-1L formation, as this type of NDH-1 was not detectable in a ΔndhP::Km mutant.
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