Identification of Novel Ssl0352 Protein (NdhS), Essential for Efficient Operation of Cyclic Electron Transport around Photosystem I, in NADPH:plastoquinone Oxidoreductase (NDH-1) Complexes of Synechocystis sp. PCC 6803

Battchikova, Natalia; Wei, Lanzhen; Du, Lei; Bersanini, Luca; Aro, Eva‐Mari; Ma, Weimin

doi:10.1074/jbc.m111.263780

Cited by 82 publications

(75 citation statements)

References 56 publications

(55 reference statements)

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“…All genes ( ndhA-C, E, G-K, M-N, S ), encoding NDH-1 core subunits (30,31), except ndhO , were downregulated in ΔrpoZ (Supplementary Table S2), and downregulation at protein level was verified for the NdhJ and NdhK proteins (Figure 3B). The ndhF4 and ndhD4 genes (but not cupB ) for the CO 2 uptake form of NDH-1 were downregulated, and also the other constitutively expressed low-affinity inorganic carbon transporter system, encoded by the bicA gene, was down.…”

Section: Resultsmentioning

confidence: 88%

The omega subunit of the RNA polymerase core directs transcription efficiency in cyanobacteria

Gunnelius

Hakkila

Kurkela

et al. 2014

Nucleic Acids Research

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The eubacterial RNA polymerase core, a transcription machinery performing DNA-dependent RNA polymerization, consists of two α subunits and β, β′ and ω subunits. An additional σ subunit is recruited for promoter recognition and transcription initiation. Cyanobacteria, a group of eubacteria characterized by oxygenic photosynthesis, have a unique composition of the RNA polymerase (RNAP) core due to splitting of the β′ subunit to N-terminal γ and C-terminal β′ subunits. The physiological roles of the small ω subunit of RNAP, encoded by the rpoZ gene, are not yet completely understood in any bacteria. We found that although ω is non-essential in cyanobacteria, it has a major impact on the overall gene expression pattern. In ΔrpoZ strain, recruitment of the primary σ factor into the RNAP holoenzyme is inefficient, which causes downregulation of highly expressed genes and upregulation of many low-expression genes. Especially, genes encoding proteins of photosynthetic carbon concentrating and carbon fixing complexes were down, and the ΔrpoZ mutant showed low light-saturated photosynthetic activity and accumulated photoprotective carotenoids and α-tocopherol. The results indicate that the ω subunit facilitates the association of the primary σ factor with the RNAP core, thereby allowing efficient transcription of highly expressed genes.

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Section: Resultsmentioning

confidence: 88%

The omega subunit of the RNA polymerase core directs transcription efficiency in cyanobacteria

Gunnelius

Hakkila

Kurkela

et al. 2014

Nucleic Acids Research

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“…The active NDH also contained NdhS (Fig. 1), the new subunit of NDH identified in Arabidopsis thaliana [18]and in Synechocystis 6803 [19] responding to the activity of NDH pathway. According to the structure similarity of NdhS with PsaE, the authors suggested that NdhS might bind with Fd which might be an electron donor for NDH.…”

Section: Discussionmentioning

confidence: 96%

Enzymatic characterization of an active NDH complex from Thermosynechococcus elongatus

et al. 2013

FEBS Letters

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a b s t r a c tAlthough type-1 NAD(P)H dehydrogenase (NDH) complex subunit constituents and physiological functions have been reported in plants and cyanobacteria, the biochemical properties of this enzyme are not clear. We used chromatographic isolation to purify and characterize a NADPH-active NDH from the cyanobacterium Thermosynechococcus elongatus. Ferredoxin (Fd) and ferredoxin-NADP + oxidoreductase (FNR) were co-eluted with NDH, implying the electron donation from NADPH to NDH via the interaction with FNR. We investigated the enzymatic properties of the complex. Furthermore, the activity is competitively inhibited by rotenone, suggesting that it possesses a quinone binding site, similar to mitochondria complex I.

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“…Cyanobacterial NADPH dehydrogenase (NDH-1) complexes localize in the thylakoid membrane (Ohkawa et al, 2001(Ohkawa et al, , 2002Zhang et al, 2004;Xu et al, 2008;Battchikova et al, 2011a) and participate in a variety of bioenergetic reactions, including respiration, cyclic electron transport around photosystem I, and CO 2 acquisition (Ogawa, 1991;Mi et al, 1992;Ohkawa et al, 2000). Structurally, the cyanobacterial NDH-1 complexes closely resemble energyconverting Complex I in eubacteria and the mitochondrial respiratory chain despite the absence in cyanobacterial genomes of homologs of the three subunits that constitute the catalytically active core of Complex I (Friedrich et al, 1995;Friedrich and Scheide, 2000;Arteni et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…NDH-CET allows optimal functioning of photosynthesis by increasing the pH gradient and supplying additional ATP for CO 2 assimilation. This function is particularly important under environmental stress conditions, such as high light (Endo et al, 1999;Battchikova et al, 2011a), in which the ATP demand is greatly increased. Moreover, the impairment of cyanobacterial NDH-CET caused by mutation of some auxiliary factors for NDH-1 complexes and Ndh subunits, such as NdhS (Battchikova et al, 2011a), results in high light-sensitive growth phenotypes.…”

Section: Introductionmentioning

confidence: 99%

Identification of a cyanobacterial CRR6 protein, Slr1097, required for efficient assembly of NDH‐1 complexes in Synechocystis sp. PCC 6803

Dai

Zhang

et al. 2013

The Plant Journal

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These authors contributed equally to this work. SUMMARYDespite significant progress in clarifying the subunit compositions and functions of the multiple NADPH dehydrogenase (NDH-1) complexes in cyanobacteria, the subunit maturation and assembly of their NDH-1 complexes are poorly understood. By transformation of wild-type cells with a transposon-tagged library, we isolated three mutants of Synechocystis sp. PCC 6803 defective in NDH-1-mediated cyclic electron transfer and unable to grow under high light conditions. All the mutants were tagged in the same slr1097 gene, encoding an unknown protein that shares significant homology with the Arabidopsis protein chlororespiratory reduction 6 (CRR6). The slr1097 product was localized in the cytoplasm and was required for efficient assembly of NDH-1 complexes. Analysis of the interaction of Slr1097 with 18 subunits of NDH-1 complexes using a yeast two-hybrid system indicated a strong interaction with NdhI but not with other Ndh subunits. Absence of Slr1097 resulted in a significant decrease of NdhI in the cytoplasm, but not of other Ndh subunits including NdhH, NdhK and NdhM; the decrease was more evident in the cytoplasm than in the thylakoid membranes. In the Δslr1097 mutant, NdhH, NdhI, NdhK and NdhM were hardly detectable in the NDH-1M complex, whereas almost half the wild-type levels of these subunits were present in NDH-1L complex; similar results were observed in the NdhI-less mutant. These results suggest that Slr1097 is involved in the maturation of NdhI, and that assembly of the NDH-1M complex is strongly dependent on this factor. Maturation of NdhI appears not to be crucial to assembly of the NDH-1L complex.

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Identification of Novel Ssl0352 Protein (NdhS), Essential for Efficient Operation of Cyclic Electron Transport around Photosystem I, in NADPH:plastoquinone Oxidoreductase (NDH-1) Complexes of Synechocystis sp. PCC 6803

Cited by 82 publications

References 56 publications

The omega subunit of the RNA polymerase core directs transcription efficiency in cyanobacteria

The omega subunit of the RNA polymerase core directs transcription efficiency in cyanobacteria

Enzymatic characterization of an active NDH complex from Thermosynechococcus elongatus

Identification of a cyanobacterial CRR6 protein, Slr1097, required for efficient assembly of NDH‐1 complexes in Synechocystis sp. PCC 6803

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