Distinct Roles of Multiple NDH-1 Complexes in the Cyanobacterial Electron Transport Network as Revealed by Kinetic Analysis of P700
 +
 Reduction in Various
 ndh
 -Deficient Mutants of
 Synechocystis
 sp. Strain PCC6803

Bernát, Gábor; Appel, Jens; Ogawa, Teruo; Rögner, Matthias

doi:10.1128/jb.00984-10

Cited by 61 publications

(60 citation statements)

References 20 publications

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“…The traces of wild-type and mutant cells were almost similar without added inhibitors (Fig. 4), as reported before for mutants of Synechocystis 6803 defective in ndhF genes (Bernát et al, 2011). The P700 + signal increased after actinic light was switched on and returned to the initial level after it was switched off.…”

Section: Psi Redox Kineticssupporting

confidence: 83%

“…As in other bacteria, it is involved in respiration, transferring electrons from carbohydrate catabolism into the plastoquinone (PQ) pool (Haimovich-Dayan et al, 2011). However, NDH1 also is involved in the cyclic electron flow around PSI (Yeremenko et al, 2005;Bernát et al, 2011). These two NDH1 functions are conserved in the chloroplastidial NDH complex that is phylogenetically derived from the cyanobacterial one (Ifuku et al, 2011).…”

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confidence: 99%

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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

Schwarz

Schubert²,

Georg

et al. 2013

Plant Physiology

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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 Dsml0013::Km mutant was almost identical to the wild type when grown under high CO 2 conditions as well as after shifts to low CO 2 conditions. However, measurements of the photosystem I redox kinetic in cells of the Dsml0013::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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Section: Psi Redox Kineticssupporting

confidence: 83%

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confidence: 99%

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

Schwarz

Schubert²,

Georg

et al. 2013

Plant Physiology

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“…Similarly, the cyanobacterium Synechocystis sp. PCC 6803 exhibits four distinct NDH1 complexes that govern PSI-mediated CEF (Battchikova et al, 2011;Bernát et al, 2011). However, the chloroplast genome of green algae lacks the genes that encode the chloroplastic Ndh complex (Maul et al, 2002;OudotLeSecq et al, 2007); thus, it has been suggested that, in green algae, CEF does not proceed through such a complex (Peltier and Cournac, 2002).…”

Section: Discussionmentioning

confidence: 99%

The Antarctic Psychrophile Chlamydomonas sp. UWO 241 Preferentially Phosphorylates a Photosystem I-Cytochrome b₆/f Supercomplex

et al. 2015

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Chlamydomonas sp. UWO 241 (UWO 241) is a psychrophilic green alga isolated from Antarctica. A unique characteristic of this algal strain is its inability to undergo state transitions coupled with the absence of photosystem II (PSII) light-harvesting complex protein phosphorylation. We show that UWO 241 preferentially phosphorylates specific polypeptides associated with an approximately 1,000-kD pigment-protein supercomplex that contains components of both photosystem I (PSI) and the cytochrome b 6 /f (Cyt b 6 /f) complex. Liquid chromatography nano-tandem mass spectrometry was used to identify three major phosphorylated proteins associated with this PSI-Cyt b 6 /f supercomplex, two 17-kD PSII subunit P-like proteins and a 70-kD ATP-dependent zinc metalloprotease, FtsH. The PSII subunit P-like protein sequence exhibited 70.6% similarity to the authentic PSII subunit P protein associated with the oxygen-evolving complex of PSII in Chlamydomonas reinhardtii. Tyrosine-146 was identified as a unique phosphorylation site on the UWO 241 PSII subunit P-like polypeptide. Assessment of PSI cyclic electron transport by in vivo P700 photooxidation and the dark relaxation kinetics of P700 + indicated that UWO 241 exhibited PSI cyclic electron transport rates that were 3 times faster and more sensitive to antimycin A than the mesophile control, Chlamydomonas raudensis SAG 49.72. The stability of the PSI-Cyt b 6 /f supercomplex was dependent upon the phosphorylation status of the PsbP-like protein and the zinc metalloprotease FtsH as well as the presence of high salt. We suggest that adaptation of UWO 241 to its unique low-temperature and high-salt environment favors the phosphorylation of a PSI-Cyt b 6 /f supercomplex to regulate PSI cyclic electron transport rather than the regulation of state transitions through the phosphorylation of PSII light-harvesting complex proteins.

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“…Four types of NDH-1 have been identified in the cyanobacterium Synechocystis sp. strain PCC 6803 (hereafter, Synechocystis 6803), and all four types of NDH-1 are involved in NDH-1-dependent cyclic electron transport (CET) around PSI (NDH-CET; Bernát et al, 2011). The NDH-CET plays an important role in coping with various environmental stresses, regardless of its elusive mechanism.…”

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confidence: 99%

Subunit Q Is Required to Stabilize the Large Complex of NADPH Dehydrogenase in Synechocystis sp. Strain PCC 6803

et al. 2015

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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 CO 2 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 CO 2 uptake. During prolonged incubation of the thylakoid membrane with n-dodecyl-b-D-maltoside at room temperature, the rest of the NDH-1L in DndhQ was disassembled completely to NDH-1M and was much faster than in the wild type. In the ndhP-deletion mutant (DndhP) background, absence of NdhQ almost completely disassembled the NDH-1L to NDH-1M, similar to the results observed in the DndhD1/DndhD2 mutant. We therefore conclude that both NdhQ and NdhP are essential to stabilize the NDH-1L complex.

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Distinct Roles of Multiple NDH-1 Complexes in the Cyanobacterial Electron Transport Network as Revealed by Kinetic Analysis of P700 ⁺ Reduction in Various ndh -Deficient Mutants of Synechocystis sp. Strain PCC6803

Cited by 61 publications

References 20 publications

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

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

The Antarctic Psychrophile Chlamydomonas sp. UWO 241 Preferentially Phosphorylates a Photosystem I-Cytochrome b₆/f Supercomplex

Subunit Q Is Required to Stabilize the Large Complex of NADPH Dehydrogenase in Synechocystis sp. Strain PCC 6803

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Distinct Roles of Multiple NDH-1 Complexes in the Cyanobacterial Electron Transport Network as Revealed by Kinetic Analysis of P700 + Reduction in Various ndh -Deficient Mutants of Synechocystis sp. Strain PCC6803

Cited by 61 publications

References 20 publications

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

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

The Antarctic Psychrophile Chlamydomonas sp. UWO 241 Preferentially Phosphorylates a Photosystem I-Cytochrome b6/f Supercomplex

Subunit Q Is Required to Stabilize the Large Complex of NADPH Dehydrogenase in Synechocystis sp. Strain PCC 6803

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Distinct Roles of Multiple NDH-1 Complexes in the Cyanobacterial Electron Transport Network as Revealed by Kinetic Analysis of P700 ⁺ Reduction in Various ndh -Deficient Mutants of Synechocystis sp. Strain PCC6803

The Antarctic Psychrophile Chlamydomonas sp. UWO 241 Preferentially Phosphorylates a Photosystem I-Cytochrome b₆/f Supercomplex