The gene encoding the NdhH subunit of type 1 NAD(P)H dehydrogenase is essential to survival of <i>Synechocystis</i> PCC6803

Pieulle, Lætitia; Guédeney, Geneviève; Cassier‐Chauvat, Corinne; Jeanjean, Robert; Chauvat, Franck; Peltier, Gilles

doi:10.1016/s0014-5793(00)02369-3

Cited by 14 publications

(13 citation statements)

References 30 publications

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“…It is unclear how the changed expression of this particular NDH subunit would influence the metabolism of M. aeruginosa, but an ndhK knock-out strain of Synechocystis sp. PCC 6803 demonstrated a decreased ability of cells to accumulate inorganic carbon (76). Such a response, where NdhK expression is low in toxic strains, but CcmK and CcmL proteins are highly expressed is consistent with the expected high-carbon requiring phenotype of microcystin-producers discussed above.…”

Section: Differential Display Between Toxic and Nontoxic Strains Of Msupporting

confidence: 76%

Comparative Protein Expression in Different Strains of the Bloom-forming Cyanobacterium Microcystis aeruginosa

Alexova

Haynes

Ferrari

et al. 2011

Molecular & Cellular Proteomics

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Toxin production in algal blooms presents a significant problem for the water industry. Of particular concern is microcystin, a potent hepatotoxin produced by the unicellular freshwater species Microcystis aeruginosa. In this study, the proteomes of six toxic and nontoxic strains of M. aeruginosa were analyzed to gain further knowledge in elucidating the role of microcystin production in this microorganism. This represents the first comparative proteomic study in a cyanobacterial species. A large diversity in the protein expression profiles of each strain was observed, with a significant proportion of the identified proteins appearing to be strain-specific. In total, 475 proteins were identified reproducibly and of these, 82 comprised the core proteome of M. aeruginosa. The expression of several hypothetical and unknown proteins, including four possible operons was confirmed. Surprisingly, no proteins were found to be produced only by toxic or nontoxic strains. Quantitative proteome analysis using the labelfree normalized spectrum abundance factor approach revealed nine proteins that were differentially expressed between toxic and nontoxic strains. These proteins participate in carbon-nitrogen metabolism and redox balance maintenance and point to an involvement of the global nitrogen regulator NtcA in toxicity. In addition, the switching of a previously inactive toxin-producing strain to microcystin synthesis is reported. Molecular & Cellular

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Section: Differential Display Between Toxic and Nontoxic Strains Of Msupporting

confidence: 76%

Comparative Protein Expression in Different Strains of the Bloom-forming Cyanobacterium Microcystis aeruginosa

Alexova

Haynes

Ferrari

et al. 2011

Molecular & Cellular Proteomics

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“…We found that the protein levels of NdhH, NdhI, and NdhK, as well as the overall activity of NDH-1, increased significantly under low CO 2 conditions. Of these, NdhH is essential for the viability of the Synechocystis PCC6803 cells (Pieulle et al 2000). Inactivation of NdhK in this bacterium decreases CO 2 uptake activity to nearly zero and NdhK mutants were unable to grow under photoheterotrophic conditions (Ogawa 1992).…”

Section: Discussionmentioning

confidence: 99%

“…This finding appears contradictory to the proposed role of NdhB in cyanobacterial inorganic carbon uptake and is inconsistent with the increase of NDH-1 activity at low CO 2 conditions. In an NdhB-defective mutant (M55), little or no NdhH, NdhJ or NdhK was found in either thylakoid or cytoplasmic membranes (Pieulle et al 2000), suggesting that the deficiency of NdhB led to an inability to assemble these subunits at thylakoid membrane. In addition, M55 cells showed severely flawed inorganic carbon uptake, which additionally suggests that inactivation of the ndhB gene in these cells may lead to disassembly of all NDH-1 complexes and the production of secondary phenotypes (Ohkawa et al 2000a).…”

Section: Discussionmentioning

confidence: 99%

Effects of Low CO2 on NAD(P)H Dehydrogenase, a Mediator of Cyclic Electron Transport Around Photosystem I in the Cyanobacterium Synechocystis PCC6803

Deng

2003

Plant and Cell Physiology

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The expression and activity of type-1 NAD(P)H dehydrogenase (NDH-1) was compared between cells of Synechocystis PCC6803 grown in high (H-cells) and low (L-cells) CO 2 conditions. Western analysis indicated that L-cells contain higher amounts of the NDH-1 subunits, NdhH, NdhI and NdhK. An NADPH-specific subcomplex of NDH-1 showed higher NADPH-nitroblue tetrazolium oxidoreductase activity in L-cells. The activities of both NADPHmenadione oxidoreductase and light-dependent NADPH oxidation driven by photosystem I were much higher in Lcells than in H-cells. The initial rate of re-reduction of P700+ following actinic light illumination in the presence of DCMU under background far-red light was enhanced in Lcells. In addition, rotenone, a specific inhibitor of NDH-1, suppressed the relative rate of post-illumination increase in Chl fluorescence of L-cells more than that of H-cells, suggesting that the involvement of NDH-1 in cyclic electron flow around photosystem I was enhanced by low CO 2 . Taken together, these results suggest that NDH-1 complex and NDH-1-mediated cyclic electron transport are stimulated by low CO 2 and function in the acclimation of cyanobacteria to low CO 2 .

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“…Gao et al (2016) identified the new NdhV subunit in Synechocystis 6803 and proposed that NdhV cooperates with NdhS to accept electrons from Fd. In addition, ndhH gene was shown to be vital to the survival of Synechocystis 6803 even under high-CO 2 growth conditions (Pieulle et al, 2000). NdhJ was found in both plasma membrane and thylakoid membranes in Synechocystis 6803 (Berger et al, 1991;Pieulle et al, 2000) and Anacystis nidulans (Dworsky et al, 1995).…”

mentioning

confidence: 99%

“…In addition, ndhH gene was shown to be vital to the survival of Synechocystis 6803 even under high-CO 2 growth conditions (Pieulle et al, 2000). NdhJ was found in both plasma membrane and thylakoid membranes in Synechocystis 6803 (Berger et al, 1991;Pieulle et al, 2000) and Anacystis nidulans (Dworsky et al, 1995). The NdhN and NdhO subunits of Synechocystis 6803 were first identified by functional proteomics approach (Prommeenate et al, 2004;Battchikova et al, 2005).…”

mentioning

confidence: 99%

Functional characterization of the subunits N, H, J, and O of the NAD(P)H dehydrogenase complexes in Synechocystis sp. strain PCC 6803

Zhong

2016

Plant Physiol.

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The cyanobacterial NAD(P)H dehydrogenase (NDH-1) complexes play crucial roles in variety of bioenergetic reactions such as respiration, CO 2 uptake, and cyclic electron transport around PSI. Recently, substantial progress has been made in identifying the composition of subunits of NDH-1 complexes. However, the localization and the physiological roles of several subunits in cyanobacteria are not fully understood. Here, by constructing fully segregated ndhN, ndhO, ndhH, and ndhJ null mutants in Synechocystis sp. strain PCC 6803, we found that deletion of ndhN, ndhH, or ndhJ but not ndhO severely impaired the accumulation of the hydrophilic subunits of the NDH-1 in the thylakoid membrane, resulting in disassembly of NDH-1MS, NDH-1MS9, as well as NDH-1L, finally causing the severe growth suppression phenotype. In contrast, deletion of NdhO affected the growth at pH 6.5 in air. In the cytoplasm, either NdhH or NdhJ deleted mutant, but neither NdhN nor NdhO deleted mutant, failed to accumulate the NDH-1 assembly intermediate consisting of NdhH, NdhJ, NdhK, and NdhM. Based on these results, we suggest that NdhN, NdhH, and NdhJ are essential for the stability and the activities of NDH-1 complexes, while NdhO for NDH-1 functions under the condition of inorganic carbon limitation in Synechocystis sp. strain PCC 6803. We discuss the roles of these subunits and propose a new NDH-1 model.

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The gene encoding the NdhH subunit of type 1 NAD(P)H dehydrogenase is essential to survival of Synechocystis PCC6803

Cited by 14 publications

References 30 publications

Comparative Protein Expression in Different Strains of the Bloom-forming Cyanobacterium Microcystis aeruginosa

Comparative Protein Expression in Different Strains of the Bloom-forming Cyanobacterium Microcystis aeruginosa

Effects of Low CO2 on NAD(P)H Dehydrogenase, a Mediator of Cyclic Electron Transport Around Photosystem I in the Cyanobacterium Synechocystis PCC6803

Functional characterization of the subunits N, H, J, and O of the NAD(P)H dehydrogenase complexes in Synechocystis sp. strain PCC 6803

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