Isolation, subunit composition and interaction of the NDH-1 complexes from <i>Thermosynechococcus elongatus</i> BP-1

Zhang, Pengpeng; Battchikova, Natalia; Paakkarinen, Virpi; Katoh, Hirokazu; Iwai, Masaru; Ikeuchi, Masahiko; Pakrasi, Himadri B.; Ogawa, Teruo; Aro, Eva‐Mari

doi:10.1042/bj20050390

Cited by 77 publications

(68 citation statements)

References 45 publications

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“…This fact suggests that the chloroplast NDH complex is similar to cyanobacterial NDH-1L that functions in respiratory and also probably PSI cyclic electron transport (2,3,8,9). Chromatography was used to show that the NDH complex purified from pea chloroplasts has a molecular mass of about 550 kDa (23). An NDH complex with a similar molecular mass was detected by native PAGE in thylakoids isolated from tobacco (25), oat (26), and barley etioplasts (27).…”

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confidence: 99%

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The Chloroplast NAD(P)H Dehydrogenase Complex Interacts with Photosystem I in Arabidopsis

Peng

Shimizu

Shikanai

2008

Journal of Biological Chemistry

159

150

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The chloroplast NAD(P)H dehydrogenase (NDH) complex is involved in photosystem I (PSI) cyclic and chlororespiratory electron transport in higher plants. Although biochemical and genetic evidence for its subunit composition has accumulated, it is not enough to explain the complexes putative activity of NAD(P)H-dependent plastoquinone reduction. We analyzed the NDH complex by using blue native PAGE and found that it interacts with PSI to form a novel supercomplex. Mutants lacking NdhL and NdhM accumulated a pigment-protein complex with a slightly lower molecular mass than that of the NDH-PSI supercomplex; this may be an intermediate supercomplex including PSI. This intermediate is unstable in mutants lacking NdhB, NdhD, or NdhF, implying that it includes some NDH subunits. Analysis of thylakoid membrane complexes using sucrose density gradient centrifugation supported the presence of the NDH-PSI supercomplex in vivo. Although the NDH complex exists as a monomer in etioplasts, it interacts with PSI to form a supercomplex within 48 h during chloroplast development. The chloroplast NAD(P)H dehydrogenase (NDH)3 complex is localized to the stroma thylakoids (1) and is involved in chlororespiration and photosystem I (PSI) cyclic electron transport in higher plants (2, 3). The NDH complex is essential for preventing over-reduction of the stroma in the pgr5 (proton gradient regulation 5) mutant, which is defective in the main pathway of PSI cyclic electron transport (4). This function suggests that NDH alleviates oxidative stress under certain conditions even in wild-type (WT) plants (3, 5). So far, 11 plastid-encoded and 4 nuclear-encoded subunits of chloroplast NDH have been identified, and all subunits are conserved in cyanobacteria. It is generally accepted that chloroplast NDH is more closely related to the cyanobacterial NDH-1 complex than to the mitochondrial complex

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“…NDH-1S associates with NDH-1M to form the NDH-1MS complex, of about 490 kDa (23). Expression of NDH-1MS can be induced under low CO 2 conditions; it is considered to be involved in CO 2 uptake (21,23). The NDH-1S complex consists of four subunits: NdhD3, NdhF3, CupA, and CupS.…”

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The Chloroplast NAD(P)H Dehydrogenase Complex Interacts with Photosystem I in Arabidopsis

Peng

Shimizu

Shikanai

2008

Journal of Biological Chemistry

159

150

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“…As a result of modification of the subunit composition, the cyanobacterial NDH complex is involved in multiple functions in respiration, PSI cyclic electron transport, and CO 2 uptake (Ohkawa et al, 2000;Shibata et al, 2001;Zhang et al, 2004Zhang et al, , 2005. In higher plants, however, both subunits are encoded by single-copy genes in the chloroplast genome (Matsubayashi et al, 1987).…”

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A Eukaryotic Factor Required for Accumulation of the Chloroplast NAD(P)H Dehydrogenase Complex in Arabidopsis

et al. 2006

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The NAD(P)H dehydrogenase (NDH) complex in chloroplasts mediates photosystem I cyclic and chlororespiratory electron transport. Eleven chloroplast genes and three nuclear genes have been identified as encoding Ndh subunits, but the entire subunit composition is still unknown. An Arabidopsis (Arabidopsis thaliana) chlororespiratory reduction (crr3) mutant was isolated based on its lack of transient increase in chlorophyll fluorescence after actinic light illumination; this was due to a specific defect in accumulation of the NDH complex. The CRR3 gene (At2g01590) encodes a novel protein containing a putative plastid-targeting signal and a transmembrane domain. Consistent with the gene structure, CRR3 localized to the membrane fraction of chloroplasts. In addition to the essential function of CRR3 in stabilizing the NDH complex, the NDH complex is also required for the accumulation of CRR3. These results suggest that CRR3 interacts with the NDH complex in the thylakoid membrane. In contrast to other subunits in the chloroplast NDH complex, CRR3 is not conserved in cyanobacteria from which the chloroplast NDH complex is believed to have originated. We propose that CRR3 is a subunit of the NDH complex, which is specific to the chloroplast.

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“…NdhA-NdhC, NdhE, NdhG-NdhO, and NdhS). In addition to these subunits, the NDH-1L complex contains NdhD1, NdhF1, NdhP, and NdhQ (Prommeenate et al, 2004;Battchikova et al, 2005Battchikova et al, , 2011bZhang et al, 2005Zhang et al, , 2014Nowaczyk et al, 2011;Wulfhorst et al, 2014;Ma and Ogawa, 2015) and is involved in respiration . NDH-1S is composed of NdhD3, NdhF3, CO 2 uptake A (CupA), and CupS (Ogawa and Mi, 2007) and is considered to be associated with NDH-1M in the cells as a functional complex NDH-1MS participating in CO 2 uptake.…”

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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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Isolation, subunit composition and interaction of the NDH-1 complexes from Thermosynechococcus elongatus BP-1

Cited by 77 publications

References 45 publications

The Chloroplast NAD(P)H Dehydrogenase Complex Interacts with Photosystem I in Arabidopsis

The Chloroplast NAD(P)H Dehydrogenase Complex Interacts with Photosystem I in Arabidopsis

A Eukaryotic Factor Required for Accumulation of the Chloroplast NAD(P)H Dehydrogenase Complex in Arabidopsis

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

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