Oxygenic photosynthesis‐specific subunits of cyanobacterial NADPH dehydrogenases

Ma, Weimin; Ogawa, Teruo

doi:10.1002/iub.1341

Cited by 38 publications

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References 59 publications

(139 reference statements)

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“…Over the past decade, a significant achievement has been made in identifying the composition and function of oxygenic photosynthesis-specific subunits from the NDH-1 complexes in cyanobacteria (for review, see Battchikova and Aro, 2007;Ogawa and Mi, 2007;Ma, 2009;Battchikova et al, 2011b;Ma and Ogawa, 2015) and higher plants (for review, see Suorsa et al, 2009;Ifuku et al, 2011;Peng et al, 2011a). Recently, a new oxygenic photosynthesis-specific subunit, NdhQ, was identified in the NDH-1L complex purified by Ni 2+ affinity chromatography from T. elongatus (Nowaczyk et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

“…Among the several copies of ndhD and ndhF genes found in cyanobacterial genomes, ndhD1 and ndhF1 show the highest homology to chloroplast ndhD and ndhF genes, respectively, and CupA and CupS subunits of the cyanobacteria have no counterparts in higher plants. These facts suggest that the structure and composition of NDH-1L, but not the NDH-1MS complex, are similar to those of the chloroplast NDH-1 complex (Battchikova and Aro, 2007;Ogawa and Mi, 2007;Shikanai, 2007;Ma, 2009;Suorsa et al, 2009;Battchikova et al, 2011b;Ifuku et al, 2011;Peng et al, 2011a;Ma and Ogawa, 2015). Despite their similarity, a large number of subunits that constitute the chloroplast NDH-1 complex, including ferredoxinbinding subcomplex subunits NdhT and NdhU and all the subunits of subcomplex B and lumen subcomplex, are absent in the cyanobacterial NDH-1L complex (Battchikova et al, 2011b;Ifuku et al, 2011;Peng et al, 2011a).…”

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confidence: 97%

“…Structurally, the cyanobacterial NDH-1 complexes closely resemble energy-converting complex I in eubacteria and the mitochondrial respiratory chain, regardless of the absence of homologs of three subunits in cyanobacterial genomes that constitute the catalytically active core of complex I (Friedrich et al, 1995;Friedrich and Scheide, 2000;Arteni et al, 2006). Over the past few years, significant achievements have been made in resolving the subunit compositions and functions of the multiple NDH-1 complexes in several cyanobacterial strains (for review, see Battchikova and Aro, 2007;Ogawa and Mi, 2007;Ma, 2009;Battchikova et al, 2011b;Ma and Ogawa, 2015). Four types of NDH-1 have been identified in the cyanobacterium Synechocystis sp.…”

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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.…”

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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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confidence: 99%

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confidence: 97%

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

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“…Cyanobacterial NDH-1 complexes have multiple functions because of the diversity of the complexes based on their different subunits composition. Although great progress has been made in revealing the functions of novel subunits of NDH-1, the localization and the function of several subunits still need to be elucidated (Ogawa and Mi, 2007;Battchikova et al, 2011a;Ma and Ogawa, 2015). The NdhN and NdhO subunits exclusively exist in oxygenic photosynthetic organisms (Prommeenate et al, 2004;Rumeau et al, 2005).…”

Section: Analyses Of Ndh-1 Assembly Intermediates Under Various Mutanmentioning

confidence: 99%

Functional characterization of the subunits N, H, J, and O of the NAD(P)H dehydrogenase complexes in Synechocystis sp. strain PCC 6803

Zhong

2016

Plant Physiol.

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The cyanobacterial NAD(P)H dehydrogenase (NDH-1) complexes play crucial roles in variety of bioenergetic reactions such as respiration, CO 2 uptake, and cyclic electron transport around PSI. Recently, substantial progress has been made in identifying the composition of subunits of NDH-1 complexes. However, the localization and the physiological roles of several subunits in cyanobacteria are not fully understood. Here, by constructing fully segregated ndhN, ndhO, ndhH, and ndhJ null mutants in Synechocystis sp. strain PCC 6803, we found that deletion of ndhN, ndhH, or ndhJ but not ndhO severely impaired the accumulation of the hydrophilic subunits of the NDH-1 in the thylakoid membrane, resulting in disassembly of NDH-1MS, NDH-1MS9, as well as NDH-1L, finally causing the severe growth suppression phenotype. In contrast, deletion of NdhO affected the growth at pH 6.5 in air. In the cytoplasm, either NdhH or NdhJ deleted mutant, but neither NdhN nor NdhO deleted mutant, failed to accumulate the NDH-1 assembly intermediate consisting of NdhH, NdhJ, NdhK, and NdhM. Based on these results, we suggest that NdhN, NdhH, and NdhJ are essential for the stability and the activities of NDH-1 complexes, while NdhO for NDH-1 functions under the condition of inorganic carbon limitation in Synechocystis sp. strain PCC 6803. We discuss the roles of these subunits and propose a new NDH-1 model.

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Membrane‐Bound Protein Complexes for Photosynthesis and Respiration in Cyanobacteria

Nagarajan

Pakrasi

2016

Encyclopedia of Life Sciences

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Cyanobacteria are the evolutionarily oldest organisms with the capability of evolving oxygen, giving rise to the present day atmosphere. These prokaryotic microorganisms have the unique ability to perform oxygenic photosynthesis and respiration in the same cellular compartment. Some cyanobacteria can also fix atmospheric nitrogen alongside oxygenic photosynthesis and respiration. The redox components of these electron transport pathways are known to intersect in cyanobacteria. Majority of the energy‐intensive processes occur in specialised membranes known as thylakoids. The coexistence of such remarkably complex metabolic pathways in a single cyanobacterial cell provides them with the potential to thrive in a wide variety of ecosystems. This metabolic complexity has sparked significant interest towards cyanobacterial research for the production of various high‐value compounds with applications in the food, feed and fuel industry. Key Concepts Cyanobacteria are the only prokaryotic microorganisms with the extraordinary capability of converting sunlight to chemical energy and evolving molecular oxygen as a byproduct. Complex metabolic processes such as photosynthesis and respiration coexist and predominantly occur in highly specialised thylakoid membranes. The photosynthetic and respiratory electron transport chain shares several components between these processes, a situation unique to oxygenic photosynthetic organisms. In ambient light conditions, photosynthetic electron transport chain has a much higher capacity for ATP synthesis than respiration.

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Oxygenic photosynthesis‐specific subunits of cyanobacterial NADPH dehydrogenases

Cited by 38 publications

References 59 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

Functional characterization of the subunits N, H, J, and O of the NAD(P)H dehydrogenase complexes in Synechocystis sp. strain PCC 6803

Membrane‐Bound Protein Complexes for Photosynthesis and Respiration in Cyanobacteria

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