NADP-Malate Dehydrogenase from Unicellular Green Alga Chlamydomonas reinhardtii. A First Step toward Redox Regulation?
The determinants of the thioredoxin (TRX)-dependent redox regulation of the chloroplastic NADP-malate dehydrogenase (NADP-MDH) from the eukaryotic green alga Chlamydomonas reinhardtii have been investigated using site-directed mutagenesis. The results indicate that a single C-terminal disulfide is r...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2005-02, Vol.137 (2), p.514-521 |
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| creator | Lemaire, Stéphane D. Alberto Quesada Faustino Merchan Juan Manuel Corral Maria Isabel Igeno Keryer, Eliane Emmanuelle Issakidis-Bourguet Hirasawa, Masakazu Knaff, David B. Miginiac-Maslow, Myroslawa |
| description | The determinants of the thioredoxin (TRX)-dependent redox regulation of the chloroplastic NADP-malate dehydrogenase (NADP-MDH) from the eukaryotic green alga Chlamydomonas reinhardtii have been investigated using site-directed mutagenesis. The results indicate that a single C-terminal disulfide is responsible for this regulation. The redox midpoint potential of this disulfide is less negative than that of the higher plant enzyme. The regulation is of an all-or-nothing type, lacking the fine-tuning provided by the second N-terminal disulfide found only in NADP-MDH from higher plants. The decreased stability of specific cysteine/alanine mutants is consistent with the presence of a structural disulfide formed by two cysteine residues that are not involved in regulation of activity. Measurements of the ability of C. reinhardtii thioredoxin f (TRX f) to activate wild-type and site-directed mutants of sorghum (Sorghum vulgare) NADP-MDH suggest that the algal TRX f has a redox midpoint potential that is less negative than most those of higher plant TRXs f. These results are discussed from an evolutionary point of view. |
| doi_str_mv | 10.1104/pp.104.052670 |
| format | Article |
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The redox midpoint potential of this disulfide is less negative than that of the higher plant enzyme. The regulation is of an all-or-nothing type, lacking the fine-tuning provided by the second N-terminal disulfide found only in NADP-MDH from higher plants. The decreased stability of specific cysteine/alanine mutants is consistent with the presence of a structural disulfide formed by two cysteine residues that are not involved in regulation of activity. Measurements of the ability of C. reinhardtii thioredoxin f (TRX f) to activate wild-type and site-directed mutants of sorghum (Sorghum vulgare) NADP-MDH suggest that the algal TRX f has a redox midpoint potential that is less negative than most those of higher plant TRXs f. These results are discussed from an evolutionary point of view.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.104.052670</identifier><identifier>PMID: 15579663</identifier><language>eng</language><publisher>United States: American Society of Plant Biologists</publisher><subject>Algae ; Allosteric regulation ; Amino Acid Sequence ; Animals ; Chlamydomonas reinhardtii ; Chlamydomonas reinhardtii - enzymology ; Chloroplasts ; Dehydrogenases ; Disulfides ; Enzyme Activation ; Enzyme Stability ; Enzymes ; Focus Issue on Chlamydomonas ; Gene Expression ; Kinetics ; Malate Dehydrogenase (NADP+) ; Malate Dehydrogenase - chemistry ; Malate Dehydrogenase - metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Physiological regulation ; Protein Conformation ; Sorghum ; Sorghum vulgare ; Thioredoxin ; Time Factors</subject><ispartof>Plant physiology (Bethesda), 2005-02, Vol.137 (2), p.514-521</ispartof><rights>Copyright 2005 American Society of Plant Biologists</rights><rights>Copyright © 2005, American Society of Plant Biologists 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c473t-c7c818e52249753f4a120a46ec143baf8d6dc3a4a674c47a608ce87192fed1623</citedby><cites>FETCH-LOGICAL-c473t-c7c818e52249753f4a120a46ec143baf8d6dc3a4a674c47a608ce87192fed1623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4629693$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4629693$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15579663$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lemaire, Stéphane D.</creatorcontrib><creatorcontrib>Alberto Quesada</creatorcontrib><creatorcontrib>Faustino Merchan</creatorcontrib><creatorcontrib>Juan Manuel Corral</creatorcontrib><creatorcontrib>Maria Isabel Igeno</creatorcontrib><creatorcontrib>Keryer, Eliane</creatorcontrib><creatorcontrib>Emmanuelle Issakidis-Bourguet</creatorcontrib><creatorcontrib>Hirasawa, Masakazu</creatorcontrib><creatorcontrib>Knaff, David B.</creatorcontrib><creatorcontrib>Miginiac-Maslow, Myroslawa</creatorcontrib><title>NADP-Malate Dehydrogenase from Unicellular Green Alga Chlamydomonas reinhardtii. A First Step toward Redox Regulation?</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>The determinants of the thioredoxin (TRX)-dependent redox regulation of the chloroplastic NADP-malate dehydrogenase (NADP-MDH) from the eukaryotic green alga Chlamydomonas reinhardtii have been investigated using site-directed mutagenesis. The results indicate that a single C-terminal disulfide is responsible for this regulation. The redox midpoint potential of this disulfide is less negative than that of the higher plant enzyme. The regulation is of an all-or-nothing type, lacking the fine-tuning provided by the second N-terminal disulfide found only in NADP-MDH from higher plants. The decreased stability of specific cysteine/alanine mutants is consistent with the presence of a structural disulfide formed by two cysteine residues that are not involved in regulation of activity. Measurements of the ability of C. reinhardtii thioredoxin f (TRX f) to activate wild-type and site-directed mutants of sorghum (Sorghum vulgare) NADP-MDH suggest that the algal TRX f has a redox midpoint potential that is less negative than most those of higher plant TRXs f. These results are discussed from an evolutionary point of view.</description><subject>Algae</subject><subject>Allosteric regulation</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Chlamydomonas reinhardtii</subject><subject>Chlamydomonas reinhardtii - enzymology</subject><subject>Chloroplasts</subject><subject>Dehydrogenases</subject><subject>Disulfides</subject><subject>Enzyme Activation</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Focus Issue on Chlamydomonas</subject><subject>Gene Expression</subject><subject>Kinetics</subject><subject>Malate Dehydrogenase (NADP+)</subject><subject>Malate Dehydrogenase - chemistry</subject><subject>Malate Dehydrogenase - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Oxidation-Reduction</subject><subject>Physiological regulation</subject><subject>Protein Conformation</subject><subject>Sorghum</subject><subject>Sorghum vulgare</subject><subject>Thioredoxin</subject><subject>Time Factors</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkc1vEzEQxS0EoiFw5IaQT71t8Pd6L6AopQWpfAjo2XK9s4mr3fXWdlry3-MoUWkvfpbnN8-jeQi9pWRBKREfpmlRZEEkUzV5hmZUclYxKfRzNCOk3InWzQl6ldINIYRyKl6iEypl3SjFZ-ju-_LsZ_XN9jYDPoPNro1hDaNNgLsYBnw1egd9v-1txBcRYMTLfm3xatPbYdeGIRQUR_DjxsY2e7_AS3zuY8r4d4YJ53Bf3vEvaMPfcq6LT_Zh_PQavehsn-DNUefo6vzzn9WX6vLHxdfV8rJyoua5crXTVINkTDS15J2wlBErFDgq-LXtdKtax62wqhalwyqiHeiaNqyDlirG5-jjwXfaXg_QOhhztL2Zoh9s3JlgvXlaGf3GrMOdoURJLvcGp0eDGG63kLIZfNpvxI4QtsnQRlMmyirnqDqALoaUInQPn1Bi9kmZaTJ7OSRV-PePJ_tPH6MpwLsDcJNyiA91oVijGs7_AfoKmg4</recordid><startdate>20050201</startdate><enddate>20050201</enddate><creator>Lemaire, Stéphane D.</creator><creator>Alberto Quesada</creator><creator>Faustino Merchan</creator><creator>Juan Manuel Corral</creator><creator>Maria Isabel Igeno</creator><creator>Keryer, Eliane</creator><creator>Emmanuelle Issakidis-Bourguet</creator><creator>Hirasawa, Masakazu</creator><creator>Knaff, David B.</creator><creator>Miginiac-Maslow, Myroslawa</creator><general>American Society of Plant Biologists</general><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>M7N</scope><scope>5PM</scope></search><sort><creationdate>20050201</creationdate><title>NADP-Malate Dehydrogenase from Unicellular Green Alga Chlamydomonas reinhardtii. A First Step toward Redox Regulation?</title><author>Lemaire, Stéphane D. ; Alberto Quesada ; Faustino Merchan ; Juan Manuel Corral ; Maria Isabel Igeno ; Keryer, Eliane ; Emmanuelle Issakidis-Bourguet ; Hirasawa, Masakazu ; Knaff, David B. ; Miginiac-Maslow, Myroslawa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c473t-c7c818e52249753f4a120a46ec143baf8d6dc3a4a674c47a608ce87192fed1623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Algae</topic><topic>Allosteric regulation</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Chlamydomonas reinhardtii</topic><topic>Chlamydomonas reinhardtii - enzymology</topic><topic>Chloroplasts</topic><topic>Dehydrogenases</topic><topic>Disulfides</topic><topic>Enzyme Activation</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Focus Issue on Chlamydomonas</topic><topic>Gene Expression</topic><topic>Kinetics</topic><topic>Malate Dehydrogenase (NADP+)</topic><topic>Malate Dehydrogenase - chemistry</topic><topic>Malate Dehydrogenase - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Oxidation-Reduction</topic><topic>Physiological regulation</topic><topic>Protein Conformation</topic><topic>Sorghum</topic><topic>Sorghum vulgare</topic><topic>Thioredoxin</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lemaire, Stéphane D.</creatorcontrib><creatorcontrib>Alberto Quesada</creatorcontrib><creatorcontrib>Faustino Merchan</creatorcontrib><creatorcontrib>Juan Manuel Corral</creatorcontrib><creatorcontrib>Maria Isabel Igeno</creatorcontrib><creatorcontrib>Keryer, Eliane</creatorcontrib><creatorcontrib>Emmanuelle Issakidis-Bourguet</creatorcontrib><creatorcontrib>Hirasawa, Masakazu</creatorcontrib><creatorcontrib>Knaff, David B.</creatorcontrib><creatorcontrib>Miginiac-Maslow, Myroslawa</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lemaire, Stéphane D.</au><au>Alberto Quesada</au><au>Faustino Merchan</au><au>Juan Manuel Corral</au><au>Maria Isabel Igeno</au><au>Keryer, Eliane</au><au>Emmanuelle Issakidis-Bourguet</au><au>Hirasawa, Masakazu</au><au>Knaff, David B.</au><au>Miginiac-Maslow, Myroslawa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NADP-Malate Dehydrogenase from Unicellular Green Alga Chlamydomonas reinhardtii. A First Step toward Redox Regulation?</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2005-02-01</date><risdate>2005</risdate><volume>137</volume><issue>2</issue><spage>514</spage><epage>521</epage><pages>514-521</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><abstract>The determinants of the thioredoxin (TRX)-dependent redox regulation of the chloroplastic NADP-malate dehydrogenase (NADP-MDH) from the eukaryotic green alga Chlamydomonas reinhardtii have been investigated using site-directed mutagenesis. The results indicate that a single C-terminal disulfide is responsible for this regulation. The redox midpoint potential of this disulfide is less negative than that of the higher plant enzyme. The regulation is of an all-or-nothing type, lacking the fine-tuning provided by the second N-terminal disulfide found only in NADP-MDH from higher plants. The decreased stability of specific cysteine/alanine mutants is consistent with the presence of a structural disulfide formed by two cysteine residues that are not involved in regulation of activity. Measurements of the ability of C. reinhardtii thioredoxin f (TRX f) to activate wild-type and site-directed mutants of sorghum (Sorghum vulgare) NADP-MDH suggest that the algal TRX f has a redox midpoint potential that is less negative than most those of higher plant TRXs f. These results are discussed from an evolutionary point of view.</abstract><cop>United States</cop><pub>American Society of Plant Biologists</pub><pmid>15579663</pmid><doi>10.1104/pp.104.052670</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Plant physiology (Bethesda), 2005-02, Vol.137 (2), p.514-521 |
| issn | 0032-0889 1532-2548 |
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| subjects | Algae Allosteric regulation Amino Acid Sequence Animals Chlamydomonas reinhardtii Chlamydomonas reinhardtii - enzymology Chloroplasts Dehydrogenases Disulfides Enzyme Activation Enzyme Stability Enzymes Focus Issue on Chlamydomonas Gene Expression Kinetics Malate Dehydrogenase (NADP+) Malate Dehydrogenase - chemistry Malate Dehydrogenase - metabolism Molecular Sequence Data Mutagenesis, Site-Directed Oxidation-Reduction Physiological regulation Protein Conformation Sorghum Sorghum vulgare Thioredoxin Time Factors |
| title | NADP-Malate Dehydrogenase from Unicellular Green Alga Chlamydomonas reinhardtii. A First Step toward Redox Regulation? |
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