Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts

Berger, Susanne; Ellersiek, Ulrike; Westhoff, Peter; Steinmüller, Klaus

doi:10.1007/bf00195671

Cited by 78 publications

(30 citation statements)

References 57 publications

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“…However, although the polypeptide products of three ndh genes (NDH H, NDH I, NDH K) have been found in thylakoid membranes of higher plants [4,5,6] it was not known whether ndh gene products are involved in a NAD(P)H dehydrogenase complex as it is the case in bacteria, cyanobacteria or mitochondria. Further, the occurrence of a NAD(P)H dehydrogenase complex in higher plant chloroplasts was recently seriously questioned [16].…”

Section: Discussionmentioning

confidence: 99%

“…These chloroplastic genes, named ndh, have been shown to be transcribed [3] and the polypeptide products of three of them (NDH H, NDH I and NDH K) have been found in thylakoid membranes [4,5,6]. It has been suggested that ndh genes encode subunits of a chloroplastic NAD(P)H dehydrogenase complex [1] which might be involved in chlororespiration, a chloroplastic respiratory process mainly studied in the unicellular green alga Chlamydomonas [7,8].…”

Section: Introductionmentioning

confidence: 99%

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Evidence for an association of ndh B, ndh J gene products and ferredoxin‐NADP‐reductase as components of a chloroplastic NAD(P)H dehydrogenase complex

et al. 1996

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Using non-denaturing gel electrophoresis and staining with nitro-blue tetrazolium, we reveal the presence of two NAD(P)H oxidoreductase activity bands within thylakoids membranes of Solanum tuberosum L. Second dimension SDS-PAGE and Western analysis show that one of the activity bands contains several polypeptides, two of them being recognized by antibodies directed against peptides corresponding to conserved domains of chloroplastic genes products NDH B and NDH J (at 32 and 18 kDa, respectively). Both activity bands also contain a polypeptide (around 36 kDa) recognized by an antibody directed against ferredoxin-NADP+-reductase (FNR). We conclude from these results that both chloroplastic ndh B and ndh J gene products are components of a thylakoid NAD(P)H dehydrogenase complex. The association with FNR is suggested to allow the complex to use NADPH instead of NADH as a preferential substrate.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Evidence for an association of ndh B, ndh J gene products and ferredoxin‐NADP‐reductase as components of a chloroplastic NAD(P)H dehydrogenase complex

et al. 1996

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“…The location of chlororespiratory and photosynthetic electron carriers within thylakoid membranes could explain such a difference. In higher plant chloroplasts, both the Ndh complex (Berger et al, 1993;Sazanov et al, 1996;Horvath et al, 2000) and PTOX (Joët et al, 2002) have been located in stroma lamellae, i.e. in the vicinity of PS I and cyt b 6 f. On the other side, PS II reaction centers are exclusively located in grana.…”

Section: Discussionmentioning

confidence: 99%

In Vivo Interactions between Photosynthesis, Mitorespiration, and Chlororespiration in Chlamydomonas reinhardtii

et al. 2002

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Interactions between photosynthesis, mitochondrial respiration (mitorespiration), and chlororespiration have been investigated in the green alga Chlamydomonas reinhardtii using flash illumination and a bare platinum electrode. Depending on the physiological status of algae, flash illumination was found to induce either a fast (t 1/2 Ϸ 300 ms) or slow (t 1/2 Ϸ 3 s) transient inhibition of oxygen uptake. Based on the effects of the mitorespiratory inhibitors myxothiazol and salicyl hydroxamic acid (SHAM), and of propyl gallate, an inhibitor of the chlororespiratory oxidase, we conclude that the fast transient is due to the flash-induced inhibition of chlororespiration and that the slow transient is due to the flash-induced inhibition of mitorespiration. By measuring blue-green fluorescence changes, related to the redox status of the pyridine nucleotide pool, and chlorophyll fluorescence, related to the redox status of plastoquinones (PQs) in C. reinhardtii wild type and in a photosystem I-deficient mutant, we show that interactions between photosynthesis and chlororespiration are favored when PQ and pyridine nucleotide pools are reduced, whereas interactions between photosynthesis and mitorespiration are favored at more oxidized states. We conclude that the plastid oxidase, similar to the mitochondrial alternative oxidase, becomes significantly engaged when the PQ pool becomes highly reduced, and thereby prevents its over-reduction.Photosynthesis and respiration, the two major bioenergetic processes of living organisms, coexist within plant cells. Although the photosynthetic electron transport chain (ETC) is clearly restricted to chloroplasts, a respiratory ETC, originally thought to be solely located in mitochondria, has been suggested to be also present in chloroplasts (Bennoun, 1982;Peltier et al., 1987). This chloroplast-based respiration, which has been called chlororespiration to differentiate it from mitorespiration (Bennoun, 1982), probably has its origins in the cyanobacterial endosymbiotic ancestor of chloroplasts (Scherer, 1990). The concept of chlororespiration was initially proposed to account for the effects of respiratory inhibitors, and particularly of inhibitors of terminal oxidases, on photosynthesis in unicellular green algae (Bennoun, 1982). It was reported that cyanide, CO, or salicyl hydroxamic acid (SHAM) increased the redox level of the plastoquinone (PQ) pool, as measured by chlorophyll (Chl) fluorescence induction curves. In addition, flash illumination of algae was found to induce the inhibition of a respiratory process (Peltier et al., 1987). The insensitivity of the flash-induced O 2 signal to both antimycin A and SHAM, inhibitors of the mitochondrial ETC, and the requirement for PS I led to the conclusion that chlororespiration, rather than mitorespiration, was inhibited by flash excitation of PS I (Peltier et al., 1987). However, reduction of the PQ pool or inhibitions of O 2 uptake could also be explained by an inhibition of mitorespiration coupled to interactions between chloropla...

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“…Like the Ndh complex (11,38,39), At-PTOX was found mainly in stroma lamellae, indicating that chlororespiration is restricted to stroma lamellae and is absent in granal thylakoids. Previously, the involvement of a propyl gallate-sensitive PQ oxidase in chlororespiration had been evidenced in Chlamydomonas cells (24).…”

Section: Measurement Of a Ps Ii-mediated Electron Flow To At-ptox In mentioning

confidence: 99%

Involvement of a Plastid Terminal Oxidase in Plastoquinone Oxidation as Evidenced by Expression of the Arabidopsis thaliana Enzyme in Tobacco

Joët¹,

Genty²,

Josse³

et al. 2002

Journal of Biological Chemistry

152

156

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Chlororespiration has been defined as a respiratory electron transport chain in interaction with photosynthetic electron transport involving both non-photochemical reduction and oxidation of plastoquinones. Different enzymatic activities, including a plastidencoded NADH dehydrogenase complex, have been reported to be involved in the non-photochemical reduction of plastoquinones. However, the enzyme responsible for plasquinol oxidation has not yet been clearly identified. In order to determine whether the newly discovered plastid oxidase (PTOX) involved in carotenoid biosynthesis acts as a plastoquinol oxidase in higher plant chloroplasts, the Arabidopsis thaliana PTOX gene (At-PTOX) was expressed in tobacco under the control of a strong constitutive promoter. We showed that At-PTOX is functional in tobacco chloroplasts and strongly accelerates the non-photochemical reoxidation of plastoquinols; this effect was inhibited by propyl gallate, a known inhibitor of PTOX. During the dark to light induction phase of photosynthesis at low irradiances, At-PTOX drives significant electron flow to O 2 , thus avoiding over-reduction of plastoquinones, when photosynthetic CO 2 assimilation was not fully induced. We proposed that PTOX, by modulating the redox state of intersystem electron carriers, may participate in the regulation of cyclic electron flow around photosystem I.

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Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts

Cited by 78 publications

References 57 publications

Evidence for an association of ndh B, ndh J gene products and ferredoxin‐NADP‐reductase as components of a chloroplastic NAD(P)H dehydrogenase complex

Evidence for an association of ndh B, ndh J gene products and ferredoxin‐NADP‐reductase as components of a chloroplastic NAD(P)H dehydrogenase complex

In Vivo Interactions between Photosynthesis, Mitorespiration, and Chlororespiration in Chlamydomonas reinhardtii

Involvement of a Plastid Terminal Oxidase in Plastoquinone Oxidation as Evidenced by Expression of the Arabidopsis thaliana Enzyme in Tobacco

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