A Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803

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

doi:10.1104/pp.15.01796

Cited by 11 publications

(17 citation statements)

References 67 publications

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“…Electrophoresis was performed at 4°C by increasing the voltage gradually from 50 up to 200 V during the 5.5-h run. CN-PAGE was performed with 0.01% DDM and 0.025% deoxycholate additives to the cathode buffer as described previously 54,55 . The purified sample (10 µg of protein) was applied to a 0.75-mm-thick, 5-12.5% acrylamide gradient gel.…”

Section: Methodsmentioning

confidence: 99%

Structural insights into NDH-1 mediated cyclic electron transfer

et al. 2020

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NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis. Here, we report a 3.2-Å-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from the cyanobacterium Thermosynechococcus elongatus. The structure reveals three β-carotene and fifteen lipid molecules in the membrane arm of NDH-1L. Regulatory oxygenic photosynthesisspecific (OPS) subunits NdhV, NdhS and NdhO are close to the Fd-binding site whilst NdhL is adjacent to the plastoquinone (PQ) cavity, and they play different roles in PSI CET under highlight stress. NdhV assists in the binding of Fd to NDH-1L and accelerates PSI CET in response to short-term highlight exposure. In contrast, prolonged highlight irradiation switches on the expression and assembly of the NDH-1MS complex, which likely contains no NdhO to further accelerate PSI CET and reduce ROS production. We propose that this hierarchical mechanism is necessary for the survival of cyanobacteria in an aerobic environment.

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Section: Methodsmentioning

confidence: 99%

Structural insights into NDH-1 mediated cyclic electron transfer

et al. 2020

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“…After the termination of AL, P700 + was reduced transiently by electrons from the plastoquinone pool; P700 is reoxidized by the background FR. Operation of the NDH-1 complex, which transfers 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, 2014Zhao et al, , 2015Wang et al, 2016). Figure 2E shows that the reoxidation of P700 was much faster in ΔcpcG2 than in the wild type.…”

Section: Inactivation Of Cpcg2 Impairs Ndh-cet Activitymentioning

confidence: 99%

“…Under high-light conditions, the growth of NDH-CETdefective mutants, such as DndhS, is markedly slower in comparison with the wild type despite similar growth under moderate light irradiation (Battchikova et al, 2011a;Dai et al, 2013;Zhang et al, 2014;Zhao et al, 2014Zhao et al, , 2015Wang et al, 2016). To screen for NDH-CETdefective mutants, we transformed wild-type cells with a transposon-bearing library, thus tagging and inactivating many genes randomly, and then cultured the mutant cells under high-light conditions.…”

Section: Isolation Of Ndh-cet-defective Mutantsmentioning

confidence: 99%

“…To test whether the high-light-sensitive growth phenotype of the two mutants resulted from defective NDH-CET, we monitored the postillumination rise in chlorophyll (Chl) fluorescence, which has been used extensively to evaluate the NDH-CET activity in cyanobacteria (Mi et al, 1995;Deng et al, 2003a;Ma and Mi, 2005;Battchikova et al, 2011a;Dai et al, 2013;Zhang et al, 2014;Zhao et al, 2014Zhao et al, , 2015Wang et al, 2016) 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). In this method, the NDH-CET activity is manifested by a transient rise of Chl fluorescence after actinic light (AL) is turned off (the corresponding phase is shown by the red rectangle in Fig.…”

Section: Isolation Of Ndh-cet-defective Mutantsmentioning

confidence: 99%

“…In cooperation with linear electron transport, CET contributes to the formation of a proton gradient across the thylakoid membrane, which increases the production of ATP in relation to NADPH and consequently optimizes the ATP/NADPH ratio. In addition, CET plays an important role in protecting photosynthesis against various environmental stresses, such as high light (Battchikova et al, 2011a;Dai et al, 2013;Zhang et al, 2014;Zhao et al, 2014Zhao et al, , 2015Wang et al, 2016).…”

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The NDH-1L-PSI Supercomplex Is Important for Efficient Cyclic Electron Transport in Cyanobacteria

et al. 2016

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Two mutants isolated from a tagging library of Synechocystis sp. strain PCC 6803 were sensitive to high light and had a tag in sll1471 encoding CpcG2, a linker protein for photosystem I (PSI)-specific antenna. Both mutants demonstrated strongly impaired NDH-1-dependent cyclic electron transport. Blue native-polyacrylamide gel electrophoresis followed by immunoblotting and mass spectrometry analyses of the wild type and a mutant containing CpcG2 fused with yellow fluorescent protein-histidine6 indicated the presence of a novel NDH-1L-CpcG2-PSI supercomplex, which was absent in the cpcG2 deletion mutant, the PSI-less mutant, and several other strains deficient in NDH-1L and/or NDH-1M. Coimmunoprecipitation and pull-down analyses on CpcG2-yellow fluorescent protein-histidine6, using antibody against green fluorescent protein and nickel column chromatography, confirmed the association of CpcG2 with the supercomplex. Conversely, the use of antibodies against NdhH or NdhK after blue native-polyacrylamide gel electrophoresis and in coimmunoprecipitation experiments verified the necessity of CpcG2 in stabilizing the supercomplex. Furthermore, deletion of CpcG2 destabilized NDH-1L as well as its degradation product NDH-1M and significantly decreased the number of functional PSI centers, consistent with the involvement of CpcG2 in NDH-1-dependent cyclic electron transport. The CpcG2 deletion, however, had no effect on respiration. Thus, we propose that the formation of an NDH-1L-CpcG2-PSI supercomplex in cyanobacteria facilitates PSI cyclic electron transport via NDH-1L.

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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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A Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803

Cited by 11 publications

References 67 publications

Structural insights into NDH-1 mediated cyclic electron transfer

Structural insights into NDH-1 mediated cyclic electron transfer

The NDH-1L-PSI Supercomplex Is Important for Efficient Cyclic Electron Transport in Cyanobacteria

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

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