scholarly journals Evolution of an assembly factor-based subunit contributed to a novel NDH-PSI supercomplex formation in chloroplasts

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Yoshinobu Kato ◽  
Masaki Odahara ◽  
Toshiharu Shikanai
Keyword(s):  
Nadh Dehydrogenase ◽  
Common Ancestor ◽  
Electron Flow ◽  
Chain Complex ◽  
Photosynthetic Electron Transport ◽  
Mitochondrial Complex ◽  
Contact Site ◽  
Tandem Gene Duplication ◽  
Transport Chain ◽  
Assembly Factor

AbstractChloroplast NADH dehydrogenase-like (NDH) complex is structurally related to mitochondrial Complex I and forms a supercomplex with two copies of Photosystem I (the NDH-PSI supercomplex) via linker proteins Lhca5 and Lhca6. The latter was acquired relatively recently in a common ancestor of angiosperms. Here we show that NDH-dependent Cyclic Electron Flow 5 (NDF5) is an NDH assembly factor in Arabidopsis. NDF5 initiates the assembly of NDH subunits (PnsB2 and PnsB3) and Lhca6, suggesting that they form a contact site with Lhca6. Our analysis of the NDF5 ortholog in Physcomitrella and angiosperm genomes reveals the subunit PnsB2 to be newly acquired via tandem gene duplication of NDF5 at some point in the evolution of angiosperms. Another Lhca6 contact subunit, PnsB3, has evolved from a protein unrelated to NDH. The structure of the largest photosynthetic electron transport chain complex has become more complicated by acquiring novel subunits and supercomplex formation with PSI.

Rewiring photosynthesis: a photosystem I-hydrogenase chimera that makes H2in vivo

2020 ◽  
Vol 13 (9) ◽  
pp. 2903-2914 ◽  
Author(s):  
Andrey Kanygin ◽  
Yuval Milrad ◽  
Chandrasekhar Thummala ◽  
Kiera Reifschneider ◽  
Patricia Baker ◽  
...  
Keyword(s):  
Electron Transport ◽  
Hydrogen Production ◽  
Photosystem I ◽  
Electron Transport Chain ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Photosynthetic Electron Transport Chain ◽  
Transport Chain

Photosystem I-hydrogenase chimera intercepts electron flow directly from the photosynthetic electron transport chain and directs it to hydrogen production.

scholarly journals Regulation of electron transport is essential for photosystem I stability and plant growth

2019 ◽  
Author(s):  
Mattia Storti ◽  
Anna Segalla ◽  
Marco Mellon ◽  
Alessandro Alboresi ◽  
Tomas Morosinotto
Keyword(s):  
Electron Transport ◽  
Photosystem I ◽  
Nadh Dehydrogenase ◽  
Physcomitrella Patens ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Type I ◽  
Growth Reduction ◽  
Light Regimes ◽  
Photosynthetic Organisms

AbstractLife depends on the ability of photosynthetic organisms to exploit sunlight to fix carbon dioxide into biomass. Photosynthesis is modulated by pathways such as cyclic and pseudocyclic electron flow (CEF and PCEF). CEF transfers electrons from photosystem I to the plastoquinone pool according to two mechanisms, one dependent on proton gradient regulators (PGR5/PGRL1) and the other on the type I NADH dehydrogenase (NDH) complex. PCEF uses electrons from photosystem I to reduce oxygen; in several groups of photosynthetic organisms but not in angiosperms, it is sustained by flavodiiron proteins (FLVs). PGR5/PGRL1, NDH and FLVs are all active in the moss Physcomitrella patens, and mutants depleted in these proteins show phenotypes under specific light regimes. Here, we demonstrated that CEF and PCEF exhibit strong functional overlap and that when one protein component is depleted, the others can compensate for most of the missing activity. When multiple mechanisms are simultaneously inactivated, however, plants show damage to photosystem I and strong growth reduction, demonstrating that mechanisms for the modulation of photosynthetic electron transport are indispensable.

scholarly journals The Campylobacter jejuni NADH:Ubiquinone Oxidoreductase (Complex I) Utilizes Flavodoxin Rather than NADH

2007 ◽  
Vol 190 (3) ◽  
pp. 915-925 ◽  
Author(s):  
Dilan R. Weerakoon ◽  
Jonathan W. Olson
Keyword(s):  
Campylobacter Jejuni ◽  
Complex I ◽  
Nadh Dehydrogenase ◽  
Respiratory Activity ◽  
Essential Gene ◽  
Electron Flow ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
The Novel ◽  
Wild Type ◽  
Transport Chain

ABSTRACT Campylobacter jejuni encodes 12 of the 14 subunits that make up the respiratory enzyme NADH:ubiquinone oxidoreductase (also called complex I). The two nuo genes not present in C. jejuni encode the NADH dehydrogenase, and in their place in the operon are the novel genes designated Cj1575c and Cj1574c. A series of mutants was generated in which each of the 12 nuo genes (homologues to known complex I subunits) was disrupted or deleted. Each of the nuo mutants will not grow in amino acid-based medium unless supplemented with an alternative respiratory substrate such as formate. Unlike the nuo genes, Cj1574c is an essential gene and could not be disrupted unless an intact copy of the gene was provided at an unrelated site on the chromosome. A nuo deletion mutant can efficiently respire formate but is deficient in α-ketoglutarate respiratory activity compared to the wild type. In C. jejuni, α-ketoglutarate respiration is mediated by the enzyme 2-oxoglutarate:acceptor oxidoreductase; mutagenesis of this enzyme abolishes α-ketoglutarate-dependent O2 uptake and fails to reduce the electron transport chain. The electron acceptor for 2-oxoglutarate:acceptor oxidoreductase was determined to be flavodoxin, which was also determined to be an essential protein in C. jejuni. A model is presented in which CJ1574 mediates electron flow into the respiratory transport chain from reduced flavodoxin and through complex I.

Inhibition and Uncoupling of Photosynthetic Electron Transport by Diterpene Lactone Amide Derivatives

2008 ◽  
Vol 63 (3-4) ◽  
pp. 251-259 ◽  
Author(s):  
Pedro A. Castelo-Branco ◽  
Flávio J. L. dos Santos ◽  
Mayura M. M. Rubinger ◽  
Dalton L. Ferreira-Alves ◽  
Dorila Piló -Veloso ◽  
...  
Keyword(s):  
Electron Transport ◽  
Electron Transport Chain ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Acceptor Site ◽  
Enzyme Complex ◽  
Cyclic Electron Transport ◽  
Fluorescence Kinetics ◽  
Transport Chain ◽  
Amide Derivatives

Nine diterpene lactone amide derivatives 1-9 were synthesized from 6-oxovouacapan- 7β,17β-lactone, which was obtained from 6α,7β-dihydroxyvouacapan-17β-oic acid isolated from Pterodon polygalaeflorus Benth., and tested for their activity on photosynthetic electron transport. Amide derivatives 3-5 behaved as electron transport chain inhibitors; they inhibited the photophosphorylation and uncoupled non-cyclic electron transport from water to methylviologen (MV). Furthermore, 4 and 5 enhanced the basal electron rate acting as uncouplers. Compound 6 behaved as an uncoupler; it enhanced the light-activated Mg2+-ATPase and basal electron flow, without affecting the uncoupled non-cyclic electron transport. Compounds 1-2 and 7-9 were less active or inactive. Compounds 3-5 did not affect photosystem I (PSI); they inhibited photosystem II (PSII) from water to 2,6-dichlorophenol indophenol (DCPIP). Compound 4 inhibited PSII from water to silicomolybdate (SiMo), but it had no effect on the reaction from diphenylcarbazide (DPC) to DCPIP indicating that its inhibition site was at the water splitting enzyme complex (OEC). Compounds 3 and 5 inhibited PSII from water to DCPIP without any effect from water to SiMo, therefore they inhibited the acceptor site of PSII. Chlorophyll a fluorescence kinetics confirmed the behaviour of 3-5

scholarly journals Novel mitochondrial complex I-inhibiting peptides restrain NADH dehydrogenase activity

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Yao-Peng Xue ◽  
Mou-Chieh Kao ◽  
Chung-Yu Lan
Keyword(s):  
Antimicrobial Peptides ◽  
Complex I ◽  
Fungal Pathogens ◽  
Nadh Dehydrogenase ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Human Fungal Pathogen ◽  
New Class ◽  
Transport Chain ◽  
Nadh Dehydrogenases

Abstract The emergence of drug-resistant fungal pathogens is becoming increasingly serious due to overuse of antifungals. Antimicrobial peptides have potent activity against a broad spectrum of pathogens, including fungi, and are considered a potential new class of antifungals. In this study, we examined the activities of the newly designed peptides P-113Du and P-113Tri, together with their parental peptide P-113, against the human fungal pathogen Candida albicans. The results showed that these peptides inhibit mitochondrial complex I, specifically NADH dehydrogenase, of the electron transport chain. Moreover, P-113Du and P-113Tri also block alternative NADH dehydrogenases. Currently, most inhibitors of the mitochondrial complex I are small molecules or artificially-designed antibodies. Here, we demonstrated novel functions of antimicrobial peptides in inhibiting the mitochondrial complex I of C. albicans, providing insight in the development of new antifungal agents.

scholarly journals PsbQ-Like Protein 3 Functions as an Assembly Factor for the Chloroplast NADH Dehydrogenase-Like Complex in Arabidopsis

2020 ◽  
Vol 61 (7) ◽  
pp. 1252-1261
Author(s):  
Noriko Ishikawa ◽  
Yuki Yokoe ◽  
Taishi Nishimura ◽  
Takeshi Nakano ◽  
Kentaro Ifuku
Keyword(s):  
Nadh Dehydrogenase ◽  
Electron Flow ◽  
Polyacrylamide Gel Electrophoresis ◽  
Oxygen Evolving Complex ◽  
Severe Reduction ◽  
Native Polyacrylamide Gel Electrophoresis ◽  
Assembly Factor ◽  
Young Leaves ◽  
Oxygen Evolving ◽  
Blue Native

Abstract Angiosperms have three PsbQ-like (PQL) proteins in addition to the PsbQ subunit of the oxygen-evolving complex of photosystem II. Previous studies have shown that two PQL proteins, PnsL2 and PnsL3, are subunits of the chloroplast NADH dehydrogenase-like (NDH) complex involved in the photosystem I (PSI) cyclic electron flow. In addition, another PsbQ homolog, PQL3, is required for the NDH activity; however, the molecular function of PQL3 has not been elucidated. Here, we show that PQL3 is an assembly factor, particularly for the accumulation of subcomplex B (SubB) of the chloroplast NDH. In the pql3 mutant of Arabidopsis thaliana, the amounts of NDH subunits in SubB, PnsB1 and PsnB4, were decreased, causing a severe reduction in the NDH–PSI supercomplex. Analysis using blue native polyacrylamide gel electrophoresis suggested that the incorporation of PnsL3 into SubB was affected in the pql3 mutant. Unlike other PsbQ homologs, PQL3 was weakly associated with thylakoid membranes and was only partially protected from thermolysin digestion. Consistent with the function as an assembly factor, PQL3 accumulated independently in other NDH mutants, such as pnsl1-3. Furthermore, PQL3 accumulated in young leaves in a manner similar to the accumulation of CRR3, an assembly factor for SubB. These results suggest that PQL3 has developed a distinct function as an assembly factor for the NDH complex during evolution of the PsbQ protein family in angiosperms.

Reactions of Antisera to Lutein and Plastoquinone with Chloroplast Preparations and their Effects on Photosynthetic Electron Transport

1973 ◽  
Vol 28 (1-2) ◽  
pp. 36-44 ◽  
Author(s):  
Alfons Radunz ◽  
Georg H. Schmid
Keyword(s):  
Electron Transport ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Potassium Ferricyanide ◽  
Electron Donors ◽  
Hill Reaction ◽  
Photosynthetic Electron Transport Chain ◽  
Transport Chain ◽  
Pass Through ◽  
The Hill

An antiserum to lutein inhibits photosynthetic electron transport between water and potassium ferricyanide in diloroplasts from green Nicotiana tabacum var. John William’s Breadleaf. However, electron transport between diphenylcarbazide and potassium ferricyanide is not impaired. From this it is concluded that the photochemically active carotenoid should feed its electrons into the photosynthetic electron transport chain before the site from which diphenyl-carbazide donates electrons. The inhibition of the ferricyanide Hill reaction in diloroplasts by antibodies to lutein depends on the accessibility of the carotenoid antigen in the thylakoid membrane. In fresh preparations the accessibility is greater in diloroplasts in which photo- synthetic electron transport is coupled to photophosphorylation. Concomitantly the antiserum to lutein agglutinates only such chloroplast preparations in which the Hill reaction is impaired by the antiserum. An antiserum to plastoquinone inhibits ferricyanide photoreduction of diloroplasts regardless whether driven by water or diphenylcarbazide as the electron donors. Typical photosystem-I-reactions are not influenced by the antiserum. In a certain type of chloroplast preparations the antiserum does not inhibit PMS-mediated photophosphorylation inferring that plastoquinone, eventually involved in this reaction, is either not accessible to antibodies, or that this cyclic electron flow does not necessarily pass through plastoquinone.

Plant Response to Combinations of Mesotrione and Photosystem II Inhibitors

2006 ◽  
Vol 20 (1) ◽  
pp. 267-274 ◽  
Author(s):  
Julie A. Abendroth ◽  
Alex R. Martin ◽  
Fred W. Roeth
Keyword(s):  
Photosystem Ii ◽  
Joint Action ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Carotenoid Biosynthesis ◽  
Ps Ii ◽  
Whole Plant ◽  
Transport Chain ◽  
Leaf Necrosis ◽  
Plant Level

Photosystem II (PS II) inhibitors halt electron flow within the photosynthetic electron transport chain, thereby leading to increased oxidative stress. As a result, their addition to mesotrione, which inhibits carotenoid biosynthesis by inhibition of the enzyme 4-hydroxyphenylpyruvate dioxygenase (HPPD), is complementary. Field and greenhouse experiments were conducted in 2002 and 2003 to investigate the joint action of POST mesotrione plus PS II inhibitor herbicide combinations. The joint action of mesotrione plus PS II inhibitors was investigated across five plant species, three PS II inhibitors, and two moisture environments to determine their influence on the joint action response. Rates of mesotrione evaluated ranged from 4.4 to 87.6 g ai/ha alone and in combination with reduced rates of atrazine, bromoxynil, and metribuzin. In the field, all combinations of mesotrione at 8.8, 17.5, and 35.0 g/ha plus atrazine, bromoxynil, or metribuzin were synergistic for necrosis 6 d after treatment (DAT) on sunflower. Addition of atrazine at 280 g/ha to mesotrione at 8.8 g/ha increased velvetleaf leaf necrosis by 18 to 47%. In the greenhouse, the addition of bromoxynil at 70 g/ha to mesotrione at 17.5 g/ha increased leaf necrosis by 23 to 34% and biomass reduction by 38 to 47%. Synergism on Palmer amaranth occurred similarly under both normal and dry moisture environments at application. Plant height at application was found to influence detection of synergism on the whole-plant level.

scholarly journals Ndufs4 ablation decreases synaptophysin expression in hippocampus

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Subrata Kumar Shil ◽  
Yoshiteru Kagawa ◽  
Banlanjo Abdulaziz Umaru ◽  
Fumika Nanto-Hara ◽  
Hirofumi Miyazaki ◽  
...  
Keyword(s):  
Nadh Dehydrogenase ◽  
Leigh Syndrome ◽  
Mitochondrial Respiratory Chain ◽  
Mitochondrial Activity ◽  
Mitochondrial Complex ◽  
Neuronal Function ◽  
Mouse Hippocampus ◽  
Extracellular Regulated Kinase ◽  
Presynaptic Protein

AbstractAltered function of mitochondrial respiratory chain in brain cells is related to many neurodegenerative diseases. NADH Dehydrogenase (Ubiquinone) Fe-S protein 4 (Ndufs4) is one of the subunits of mitochondrial complex I and its mutation in human is associated with Leigh syndrome. However, the molecular biological role of Ndufs4 in neuronal function is poorly understood. In this study, upon Ndufs4 expression confirmation in NeuN-positive neurons, and GFAP-positive astrocytes in WT mouse hippocampus, we found significant decrease of mitochondrial respiration in Ndufs4-KO mouse hippocampus. Although there was no change in the number of NeuN positive neurons in Ndufs4-KO hippocampus, the expression of synaptophysin, a presynaptic protein, was significantly decreased. To investigate the detailed mechanism, we silenced Ndufs4 in Neuro-2a cells and we observed shorter neurite lengths with decreased expression of synaptophysin. Furthermore, western blot analysis for phosphorylated extracellular regulated kinase (pERK) revealed that Ndufs4 silencing decreases the activity of ERK signalling. These results suggest that Ndufs4-modulated mitochondrial activity may be involved in neuroplasticity via regulating synaptophysin expression.

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