Critical Roles of Subunit NuoH (ND1) in the Assembly of Peripheral Subunits with the Membrane Domain of Escherichia coli NDH-1
The bacterial proton-translocating NADH:quinone oxidoreductase (NDH-1) consists of two domains, a peripheral arm and a membrane arm. NuoH is a counterpart of ND1, which is one of seven mitochondrially encoded hydrophobic subunits, and is considered to be involved in quinone/inhibitor binding. Sequen...
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| Veröffentlicht in: | The Journal of biological chemistry 2009-04, Vol.284 (15), p.9814-9823 |
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| creator | Sinha, Prem Kumar Torres-Bacete, Jesus Nakamaru-Ogiso, Eiko Castro-Guerrero, Norma Matsuno-Yagi, Akemi Yagi, Takao |
| description | The bacterial proton-translocating NADH:quinone oxidoreductase (NDH-1) consists of two domains, a peripheral arm and a membrane arm. NuoH is a counterpart of ND1, which is one of seven mitochondrially encoded hydrophobic subunits, and is considered to be involved in quinone/inhibitor binding. Sequence comparison in a wide range of species showed that NuoH is comprehensively conserved, particularly with charged residues in the cytoplasmic side loops. We have constructed 40 mutants of 27 conserved residues predicted to be in the cytoplasmic side loops of Escherichia coli NuoH by utilizing the chromosomal DNA manipulation technique and investigated roles of these residues. Mutants of Arg37, Arg46, Asp63, Gly134, Gly145, Arg148, Glu220, and Glu228 showed low deamino-NADH-K3Fe(CN)6 reductase activity, undetectable NDH-1 in Blue Native gels, low contents of peripheral subunits (especially NuoB and NuoCD) bound to the membranes, and a significant loss of the membrane potential and proton-pumping function coupled to deamino-NADH oxidation. The results indicated that these conserved residues located in the cytoplasmic side loops are essential for the assembly of the peripheral subunits with the membrane arm. Implications for the involvement of NuoH (ND1) in maintaining the structure and function of NDH-1 are discussed. |
| doi_str_mv | 10.1074/jbc.M809468200 |
| format | Article |
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NuoH is a counterpart of ND1, which is one of seven mitochondrially encoded hydrophobic subunits, and is considered to be involved in quinone/inhibitor binding. Sequence comparison in a wide range of species showed that NuoH is comprehensively conserved, particularly with charged residues in the cytoplasmic side loops. We have constructed 40 mutants of 27 conserved residues predicted to be in the cytoplasmic side loops of Escherichia coli NuoH by utilizing the chromosomal DNA manipulation technique and investigated roles of these residues. Mutants of Arg37, Arg46, Asp63, Gly134, Gly145, Arg148, Glu220, and Glu228 showed low deamino-NADH-K3Fe(CN)6 reductase activity, undetectable NDH-1 in Blue Native gels, low contents of peripheral subunits (especially NuoB and NuoCD) bound to the membranes, and a significant loss of the membrane potential and proton-pumping function coupled to deamino-NADH oxidation. The results indicated that these conserved residues located in the cytoplasmic side loops are essential for the assembly of the peripheral subunits with the membrane arm. Implications for the involvement of NuoH (ND1) in maintaining the structure and function of NDH-1 are discussed.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M809468200</identifier><identifier>PMID: 19189973</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Cloning, Molecular ; Cytoplasm - metabolism ; DNA - chemistry ; Escherichia coli ; Escherichia coli - metabolism ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - physiology ; Immunoblotting ; Kinetics ; Membrane Proteins - chemistry ; Membrane Proteins - physiology ; Metabolism and Bioenergetics ; Models, Genetic ; Molecular Sequence Data ; Mutation ; NAD - chemistry ; Oxygen - chemistry ; Protein Conformation ; Protein Structure, Tertiary ; Quinone Reductases - chemistry ; Quinone Reductases - metabolism</subject><ispartof>The Journal of biological chemistry, 2009-04, Vol.284 (15), p.9814-9823</ispartof><rights>2009 © 2009 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>Copyright © 2009, The American Society for Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-2dcc7056ec7960b8359e6074813b7450b090c640f779d127df989026dff9f1003</citedby><cites>FETCH-LOGICAL-c520t-2dcc7056ec7960b8359e6074813b7450b090c640f779d127df989026dff9f1003</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2665103/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2665103/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19189973$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sinha, Prem Kumar</creatorcontrib><creatorcontrib>Torres-Bacete, Jesus</creatorcontrib><creatorcontrib>Nakamaru-Ogiso, Eiko</creatorcontrib><creatorcontrib>Castro-Guerrero, Norma</creatorcontrib><creatorcontrib>Matsuno-Yagi, Akemi</creatorcontrib><creatorcontrib>Yagi, Takao</creatorcontrib><title>Critical Roles of Subunit NuoH (ND1) in the Assembly of Peripheral Subunits with the Membrane Domain of Escherichia coli NDH-1</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The bacterial proton-translocating NADH:quinone oxidoreductase (NDH-1) consists of two domains, a peripheral arm and a membrane arm. NuoH is a counterpart of ND1, which is one of seven mitochondrially encoded hydrophobic subunits, and is considered to be involved in quinone/inhibitor binding. Sequence comparison in a wide range of species showed that NuoH is comprehensively conserved, particularly with charged residues in the cytoplasmic side loops. We have constructed 40 mutants of 27 conserved residues predicted to be in the cytoplasmic side loops of Escherichia coli NuoH by utilizing the chromosomal DNA manipulation technique and investigated roles of these residues. Mutants of Arg37, Arg46, Asp63, Gly134, Gly145, Arg148, Glu220, and Glu228 showed low deamino-NADH-K3Fe(CN)6 reductase activity, undetectable NDH-1 in Blue Native gels, low contents of peripheral subunits (especially NuoB and NuoCD) bound to the membranes, and a significant loss of the membrane potential and proton-pumping function coupled to deamino-NADH oxidation. The results indicated that these conserved residues located in the cytoplasmic side loops are essential for the assembly of the peripheral subunits with the membrane arm. Implications for the involvement of NuoH (ND1) in maintaining the structure and function of NDH-1 are discussed.</description><subject>Amino Acid Sequence</subject><subject>Cloning, Molecular</subject><subject>Cytoplasm - metabolism</subject><subject>DNA - chemistry</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - physiology</subject><subject>Immunoblotting</subject><subject>Kinetics</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - physiology</subject><subject>Metabolism and Bioenergetics</subject><subject>Models, Genetic</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>NAD - chemistry</subject><subject>Oxygen - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Quinone Reductases - chemistry</subject><subject>Quinone Reductases - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9v0zAUB_AIgVgZXDmCJSQEh5T3nMQ_LpOmdlCkrSDGJG5W4jiNpyQudrJpF_52XFoxOCByySGf99V7-SbJc4Q5As_fXVd6fiFA5kxQgAfJDEFkaVbgt4fJDIBiKmkhjpInIVxDfHKJj5MjlCik5Nks-bHwdrS67MgX15lAXEMup2oa7EjWk1uRN-slviV2IGNryGkIpq-6u536bLzdtsbHycNAILd2bH_Bi8h8ORiydH0Zh6M_Czpqq1tbEu06S9bLVYpPk0dN2QXz7PA-Tq7en31drNLzTx8-Lk7PU11QGFNaa82hYEZzyaASWSENi-cLzCqeF1CBBM1yaDiXNVJeN1JIoKxuGtkgQHacnOxzt1PVm1qbYYybq623fenvlCut-vvLYFu1cTeKMlYgZDHg9SHAu--TCaPqbdCm6-KVbgqKccScAvsvpLvakO8S53uovQvBm-b3Nghqh1TsVt13Gwde_HnDPT-UGcGrPWjtpr213qjKuvjXe0VFrrBQUmAe1cu9akqnyo23QV1dUsAMkGFWCBmF2AsTG7mxxqugrRm0qWOmHlXt7L92_Am7hcZM</recordid><startdate>20090410</startdate><enddate>20090410</enddate><creator>Sinha, Prem Kumar</creator><creator>Torres-Bacete, Jesus</creator><creator>Nakamaru-Ogiso, Eiko</creator><creator>Castro-Guerrero, Norma</creator><creator>Matsuno-Yagi, Akemi</creator><creator>Yagi, Takao</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090410</creationdate><title>Critical Roles of Subunit NuoH (ND1) in the Assembly of Peripheral Subunits with the Membrane Domain of Escherichia coli NDH-1</title><author>Sinha, Prem Kumar ; 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NuoH is a counterpart of ND1, which is one of seven mitochondrially encoded hydrophobic subunits, and is considered to be involved in quinone/inhibitor binding. Sequence comparison in a wide range of species showed that NuoH is comprehensively conserved, particularly with charged residues in the cytoplasmic side loops. We have constructed 40 mutants of 27 conserved residues predicted to be in the cytoplasmic side loops of Escherichia coli NuoH by utilizing the chromosomal DNA manipulation technique and investigated roles of these residues. Mutants of Arg37, Arg46, Asp63, Gly134, Gly145, Arg148, Glu220, and Glu228 showed low deamino-NADH-K3Fe(CN)6 reductase activity, undetectable NDH-1 in Blue Native gels, low contents of peripheral subunits (especially NuoB and NuoCD) bound to the membranes, and a significant loss of the membrane potential and proton-pumping function coupled to deamino-NADH oxidation. 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| subjects | Amino Acid Sequence Cloning, Molecular Cytoplasm - metabolism DNA - chemistry Escherichia coli Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - physiology Immunoblotting Kinetics Membrane Proteins - chemistry Membrane Proteins - physiology Metabolism and Bioenergetics Models, Genetic Molecular Sequence Data Mutation NAD - chemistry Oxygen - chemistry Protein Conformation Protein Structure, Tertiary Quinone Reductases - chemistry Quinone Reductases - metabolism |
| title | Critical Roles of Subunit NuoH (ND1) in the Assembly of Peripheral Subunits with the Membrane Domain of Escherichia coli NDH-1 |
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