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NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO(2) Uptake in Synechocystis sp. Strain PCC 6803
The cyanobacterial type I NAD(P)H dehydrogenase (NDH-1) complexes play a crucial role in a variety of bioenergetic reactions such as respiration, CO(2) uptake, and cyclic electron transport around photosystem I. Two types of NDH-1 complexes, NDH-1MS and NDH-1MS′, are involved in the CO(2) uptake sys...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4786724/ https://www.ncbi.nlm.nih.gov/pubmed/26703473 http://dx.doi.org/10.1074/jbc.M115.698084 |
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author | He, Zhihui Xu, Min Wu, Yaozong Lv, Jing Fu, Pengcheng Mi, Hualing |
author_facet | He, Zhihui Xu, Min Wu, Yaozong Lv, Jing Fu, Pengcheng Mi, Hualing |
author_sort | He, Zhihui |
collection | PubMed |
description | The cyanobacterial type I NAD(P)H dehydrogenase (NDH-1) complexes play a crucial role in a variety of bioenergetic reactions such as respiration, CO(2) uptake, and cyclic electron transport around photosystem I. Two types of NDH-1 complexes, NDH-1MS and NDH-1MS′, are involved in the CO(2) uptake system. However, the composition and function of the complexes still remain largely unknown. Here, we found that deletion of ndhM caused inactivation of NDH-1-dependent cyclic electron transport around photosystem I and abolishment of CO(2) uptake, resulting in a lethal phenotype under air CO(2) condition. The mutation of NdhM abolished the accumulation of the hydrophilic subunits of the NDH-1, such as NdhH, NdhI, NdhJ, and NdhK, in the thylakoid membrane, resulting in disassembly of NDH-1MS and NDH-1MS′ as well as NDH-1L. In contrast, the accumulation of the hydrophobic subunits was not affected in the absence of NdhM. In the cytoplasm, the NDH-1 subcomplex assembly intermediates including NdhH and NdhK were seriously affected in the ΔndhM mutant but not in the NdhI-deleted mutant ΔndhI. In vitro protein interaction analysis demonstrated that NdhM interacts with NdhK, NdhH, NdhI, and NdhJ but not with other hydrophilic subunits of the NDH-1 complex. These results suggest that NdhM localizes in the hydrophilic subcomplex of NDH-1 complexes as a core subunit and is essential for the function of NDH-1MS and NDH-1MS′ involved in CO(2) uptake in Synechocystis sp. strain PCC 6803. |
format | Online Article Text |
id | pubmed-4786724 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-47867242016-03-16 NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO(2) Uptake in Synechocystis sp. Strain PCC 6803 He, Zhihui Xu, Min Wu, Yaozong Lv, Jing Fu, Pengcheng Mi, Hualing J Biol Chem Bioenergetics The cyanobacterial type I NAD(P)H dehydrogenase (NDH-1) complexes play a crucial role in a variety of bioenergetic reactions such as respiration, CO(2) uptake, and cyclic electron transport around photosystem I. Two types of NDH-1 complexes, NDH-1MS and NDH-1MS′, are involved in the CO(2) uptake system. However, the composition and function of the complexes still remain largely unknown. Here, we found that deletion of ndhM caused inactivation of NDH-1-dependent cyclic electron transport around photosystem I and abolishment of CO(2) uptake, resulting in a lethal phenotype under air CO(2) condition. The mutation of NdhM abolished the accumulation of the hydrophilic subunits of the NDH-1, such as NdhH, NdhI, NdhJ, and NdhK, in the thylakoid membrane, resulting in disassembly of NDH-1MS and NDH-1MS′ as well as NDH-1L. In contrast, the accumulation of the hydrophobic subunits was not affected in the absence of NdhM. In the cytoplasm, the NDH-1 subcomplex assembly intermediates including NdhH and NdhK were seriously affected in the ΔndhM mutant but not in the NdhI-deleted mutant ΔndhI. In vitro protein interaction analysis demonstrated that NdhM interacts with NdhK, NdhH, NdhI, and NdhJ but not with other hydrophilic subunits of the NDH-1 complex. These results suggest that NdhM localizes in the hydrophilic subcomplex of NDH-1 complexes as a core subunit and is essential for the function of NDH-1MS and NDH-1MS′ involved in CO(2) uptake in Synechocystis sp. strain PCC 6803. American Society for Biochemistry and Molecular Biology 2016-03-11 2015-12-24 /pmc/articles/PMC4786724/ /pubmed/26703473 http://dx.doi.org/10.1074/jbc.M115.698084 Text en © 2016 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0) . |
spellingShingle | Bioenergetics He, Zhihui Xu, Min Wu, Yaozong Lv, Jing Fu, Pengcheng Mi, Hualing NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO(2) Uptake in Synechocystis sp. Strain PCC 6803 |
title | NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO(2) Uptake in Synechocystis sp. Strain PCC 6803
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title_full | NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO(2) Uptake in Synechocystis sp. Strain PCC 6803
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title_fullStr | NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO(2) Uptake in Synechocystis sp. Strain PCC 6803
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title_full_unstemmed | NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO(2) Uptake in Synechocystis sp. Strain PCC 6803
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title_short | NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO(2) Uptake in Synechocystis sp. Strain PCC 6803
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title_sort | ndhm subunit is required for the stability and the function of nad(p)h dehydrogenase complexes involved in co(2) uptake in synechocystis sp. strain pcc 6803 |
topic | Bioenergetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4786724/ https://www.ncbi.nlm.nih.gov/pubmed/26703473 http://dx.doi.org/10.1074/jbc.M115.698084 |
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