NdhP Is an Exclusive Subunit of Large Complex of NADPH Dehydrogenase Essential to Stabilize the Complex in Synechocystis sp. Strain PCC 6803

Zhang, Jingsong; Feng, Gao; Zhao, Jing–Shan; Ogawa, Teruo; Wang, Quanxi; Ma, Weimin

doi:10.1074/jbc.m114.553404

Cited by 37 publications

(51 citation statements)

References 56 publications

(65 reference statements)

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“…This approach has been extensively used to monitor NDH-CET activity in cyanobacteria Deng et al, 2003;Ma and Mi, 2005;Battchikova et al, 2011a;Dai et al, 2013;Zhang et al, 2014;Zhao et al, 2014) and higher plants (Burrows et al, 1998;Shikanai et al, 1998;Hashimoto et al, 2003;Wang et al, 2006;Peng et al, 2009Peng et al, , 2011bPeng et al, , 2012Sirpiö et al, 2009;Yamamoto et al, 2011;Armbruster et al, 2013). As shown in Figure 1B, the NDH-CET activity in both mutants was lower than that in the wild type as judged by the height and relative rate of postillumination increase in Chl fluorescence.…”

Section: Isolation Of Ndh-cet-defective Mutantsmentioning

confidence: 99%

“…The NDH-CET has a protective role against high light stress in cyanobacteria (Battchikova et al, 2011a;Dai et al, 2013;Zhang et al, 2014;Zhao et al, 2014) and higher plants (Endo et al, 1999). Under high light conditions, therefore, the growth of NDH-CET-defective mutants is markedly retarded compared with the wild type, despite similar growth under moderate light irradiation.…”

Section: Isolation Of Ndh-cet-defective Mutantsmentioning

confidence: 99%

“…Operation of the NDH-1 complexes, which transfer electrons from the reduced cytoplasmic pool to plastoquinone, hinders the reoxidation of P700 (Shikanai et al, 1998;Battchikova et al, 2011a;Dai et al, 2013;Zhang et al, 2014;Zhao et al, 2014). The reoxidation of P700 was evidently faster in ΔndhQ compared with the wild type but was much slower than in M55 (Fig.…”

mentioning

confidence: 98%

“…The NDH-CET plays an important role in coping with various environmental stresses, regardless of its elusive mechanism. For example, this function can greatly alleviate high light-sensitive growth phenotypes (Endo et al, 1999;Battchikova et al, 2011a;Dai et al, 2013;Zhang et al, 2014;Zhao et al, 2014). Therefore, high light strategy can help in identifying the proteins essential to NDH-CET.…”

mentioning

confidence: 99%

“…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.…”

mentioning

confidence: 99%

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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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Section: Isolation Of Ndh-cet-defective Mutantsmentioning

confidence: 99%

Section: Isolation Of Ndh-cet-defective Mutantsmentioning

confidence: 99%

mentioning

confidence: 98%

mentioning

confidence: 99%

mentioning

confidence: 99%

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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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Oxygenic photosynthesis‐specific subunits of cyanobacterial NADPH dehydrogenases

Ogawa

2015

IUBMB Life

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Cyanobacterial NADPH dehydrogenase (NDH-1) or NDH-1-like complex is localized in the thylakoid membrane and participates in a variety of bioenergetic reactions, including respiration, cyclic electron transport around photosystem I and CO 2 uptake. Over the past decade, a significant achievement has been made in identifying seven oxygenic photosynthesisspecific (OPS) subunits of NDH-1 enzyme, NdhL to NdhQ and NdhS, in several cyanobacterial strains. Six of them are also found in higher plants but not in nonphototrophs. This indicates an exclusive existence of these OPS Ndh subunits in oxygenic photosynthetic organisms and suggested certain role of cyanobacterial and chloroplastic NDH-1 in photosynthetic reactions. In this review, we describe these seven OPS subunits of cyanobacterial NDH-1, focusing on their identification, localization, function, and evolution from cyanobacteria to higher plants. A crucial role of these OPS subunits on the function of cyanobacterial NDH-1 is proposed. V C 2015 IUBMB Life, 67(1):3-8, 2015

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NDH‐1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria

et al. 2023

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Cyanobacterial NdhM, an oxygenic photosynthesis‐specific NDH‐1 subunit, has been found to be essential for the formation of a large complex of NDH‐1 (NDH‐1L). The cryo‐electron microscopic (cryo‐EM) structure of NdhM from Thermosynechococcus elongatus showed that the N‐terminus of NdhM contains three β‐sheets, while two α‐helixes are present in the middle and C‐terminal part of NdhM. Here, we obtained a mutant of the unicellular cyanobacterium Synechocystis 6803 expressing a C‐terminal truncated NdhM subunit designated NdhMΔC. Accumulation and activity of NDH‐1 were not affected in NdhMΔC under normal growth conditions. However, the NDH‐1 complex with truncated NdhM is unstable under stress. Immunoblot analyses showed that the assembly process of the cyanobacterial NDH‐1L hydrophilic arm was not affected in the NdhMΔC mutant even under high temperature. Thus, our results indicate that NdhM can bind to the NDH‐1 complex without its C‐terminal α‐helix, but the interaction is weakened. NDH‐1L with truncated NdhM is more prone to dissociation, and this is particularly evident under stress conditions.

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NdhP Is an Exclusive Subunit of Large Complex of NADPH Dehydrogenase Essential to Stabilize the Complex in Synechocystis sp. Strain PCC 6803

Cited by 37 publications

References 56 publications

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

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

Oxygenic photosynthesis‐specific subunits of cyanobacterial NADPH dehydrogenases

NDH‐1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria

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