Maize recombinant non-C4 NADP-malic enzyme: A novel dimeric malic enzyme with high specific activity
Among the different isoforms of NADP-malic enzyme (NADP-ME) involved in a wide range of metabolic pathways in plants, the NADP-ME that participates in C4-photosynthesis is the most studied. In the present work, the expression in E. coli of a cDNA encoding for a maize non-photosynthetic NADP-ME is pr...
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| Veröffentlicht in: | Plant molecular biology 2004-05, Vol.55 (1), p.97-107 |
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| creator | Saigo, M Bologna, F.P Maurino, V.G Detarsio, E Andreo, C.S Drincovich, M.F |
| description | Among the different isoforms of NADP-malic enzyme (NADP-ME) involved in a wide range of metabolic pathways in plants, the NADP-ME that participates in C4-photosynthesis is the most studied. In the present work, the expression in E. coli of a cDNA encoding for a maize non-photosynthetic NADP-ME is presented. The recombinant NADP-ME thus obtained presents kinetic and structural properties different from the enzyme previously purified from etiolated leaves and roots. Moreover, the recombinant non-photosynthetic NADP-ME presents very high intrinsic NADP-ME activity, which is unexpected for a non-C4 NADP-ME. Using antibodies against this recombinant enzyme, an immunoreactive band of 66 kDa is detected in different maize tissues indicating that the 66 kDa-NADP-ME is in fact a protein expressed in vivo. The recombinant NADP-ME assembles as a dimer, although the results obtained indicate that a higher molecular mass oligomeric state of the enzyme is found in maize roots in vivo. In this way, maize presents at least three NADP-ME isoforms: a 72 kDa constitutive form (previously characterized); the novel non-photosynthetic 66 kDa isoform characterized in this work (which is the product of the ZmChlMe2 gene and the likely precursor to the evolution of the photosynthetic C4 NADP-ME) and the 62 kDa isoform (implicated in C4 photosynthesis). The contribution of the present work anticipates further studies concerning the equilibrium between the oligomeric states of the NADP-ME isoforms and the evolution towards the C4 isoenzyme in maize. |
| doi_str_mv | 10.1007/s11103-004-0472-z |
| format | Article |
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In the present work, the expression in E. coli of a cDNA encoding for a maize non-photosynthetic NADP-ME is presented. The recombinant NADP-ME thus obtained presents kinetic and structural properties different from the enzyme previously purified from etiolated leaves and roots. Moreover, the recombinant non-photosynthetic NADP-ME presents very high intrinsic NADP-ME activity, which is unexpected for a non-C4 NADP-ME. Using antibodies against this recombinant enzyme, an immunoreactive band of 66 kDa is detected in different maize tissues indicating that the 66 kDa-NADP-ME is in fact a protein expressed in vivo. The recombinant NADP-ME assembles as a dimer, although the results obtained indicate that a higher molecular mass oligomeric state of the enzyme is found in maize roots in vivo. In this way, maize presents at least three NADP-ME isoforms: a 72 kDa constitutive form (previously characterized); the novel non-photosynthetic 66 kDa isoform characterized in this work (which is the product of the ZmChlMe2 gene and the likely precursor to the evolution of the photosynthetic C4 NADP-ME) and the 62 kDa isoform (implicated in C4 photosynthesis). The contribution of the present work anticipates further studies concerning the equilibrium between the oligomeric states of the NADP-ME isoforms and the evolution towards the C4 isoenzyme in maize.</description><identifier>ISSN: 0167-4412</identifier><identifier>EISSN: 1573-5028</identifier><identifier>DOI: 10.1007/s11103-004-0472-z</identifier><identifier>PMID: 15604667</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Blotting, Western ; Cloning, Molecular ; complementary DNA ; Corn ; Dimerization ; DNA, Complementary - chemistry ; DNA, Complementary - genetics ; E coli ; enzyme activity ; Escherichia coli ; gene expression ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Plant ; immunohistochemistry ; Isoenzymes - chemistry ; Isoenzymes - genetics ; Isoenzymes - metabolism ; isozymes ; Kinetics ; leaves ; Malate Dehydrogenase - chemistry ; Malate Dehydrogenase - genetics ; Malate Dehydrogenase - metabolism ; malic enzyme ; Molecular Sequence Data ; Molecular Weight ; nucleotide sequences ; Photosynthesis ; protein quaternary structure ; recombinant proteins ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Roots ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; substrate specificity ; Zea mays ; Zea mays - enzymology ; Zea mays - genetics</subject><ispartof>Plant molecular biology, 2004-05, Vol.55 (1), p.97-107</ispartof><rights>Kluwer Academic Publishers 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c263t-ebc9a137e19f20e84d2d9771a5923da8cf6f10d61d3959f3601ca1db7da3a9fd3</citedby><cites>FETCH-LOGICAL-c263t-ebc9a137e19f20e84d2d9771a5923da8cf6f10d61d3959f3601ca1db7da3a9fd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15604667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Saigo, M</creatorcontrib><creatorcontrib>Bologna, F.P</creatorcontrib><creatorcontrib>Maurino, V.G</creatorcontrib><creatorcontrib>Detarsio, E</creatorcontrib><creatorcontrib>Andreo, C.S</creatorcontrib><creatorcontrib>Drincovich, M.F</creatorcontrib><title>Maize recombinant non-C4 NADP-malic enzyme: A novel dimeric malic enzyme with high specific activity</title><title>Plant molecular biology</title><addtitle>Plant Mol Biol</addtitle><description>Among the different isoforms of NADP-malic enzyme (NADP-ME) involved in a wide range of metabolic pathways in plants, the NADP-ME that participates in C4-photosynthesis is the most studied. In the present work, the expression in E. coli of a cDNA encoding for a maize non-photosynthetic NADP-ME is presented. The recombinant NADP-ME thus obtained presents kinetic and structural properties different from the enzyme previously purified from etiolated leaves and roots. Moreover, the recombinant non-photosynthetic NADP-ME presents very high intrinsic NADP-ME activity, which is unexpected for a non-C4 NADP-ME. Using antibodies against this recombinant enzyme, an immunoreactive band of 66 kDa is detected in different maize tissues indicating that the 66 kDa-NADP-ME is in fact a protein expressed in vivo. The recombinant NADP-ME assembles as a dimer, although the results obtained indicate that a higher molecular mass oligomeric state of the enzyme is found in maize roots in vivo. In this way, maize presents at least three NADP-ME isoforms: a 72 kDa constitutive form (previously characterized); the novel non-photosynthetic 66 kDa isoform characterized in this work (which is the product of the ZmChlMe2 gene and the likely precursor to the evolution of the photosynthetic C4 NADP-ME) and the 62 kDa isoform (implicated in C4 photosynthesis). The contribution of the present work anticipates further studies concerning the equilibrium between the oligomeric states of the NADP-ME isoforms and the evolution towards the C4 isoenzyme in maize.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Blotting, Western</subject><subject>Cloning, Molecular</subject><subject>complementary DNA</subject><subject>Corn</subject><subject>Dimerization</subject><subject>DNA, Complementary - chemistry</subject><subject>DNA, Complementary - genetics</subject><subject>E coli</subject><subject>enzyme activity</subject><subject>Escherichia coli</subject><subject>gene expression</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Gene Expression Regulation, Plant</subject><subject>immunohistochemistry</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - genetics</subject><subject>Isoenzymes - metabolism</subject><subject>isozymes</subject><subject>Kinetics</subject><subject>leaves</subject><subject>Malate Dehydrogenase - chemistry</subject><subject>Malate Dehydrogenase - genetics</subject><subject>Malate Dehydrogenase - metabolism</subject><subject>malic enzyme</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>nucleotide sequences</subject><subject>Photosynthesis</subject><subject>protein quaternary structure</subject><subject>recombinant proteins</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Roots</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>substrate specificity</subject><subject>Zea mays</subject><subject>Zea mays - enzymology</subject><subject>Zea mays - genetics</subject><issn>0167-4412</issn><issn>1573-5028</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkEtvUzEQRi0EomnhB7ABiwU7w8y1r33NLgoUkMpDgq4tx4_G1X2k9k1R8utxlUggViPNd77R6BDyAuEtAqh3BRGBMwDBQKiGHR6RBbaKsxaa7jFZAErFhMDmjJyXcgtQW1w-JWfYShBSqgXxX206BJqDm4Z1Gu0403Ea2UrQb8sPP9hg--RoGA_7Ibyny5rdh576NIRc9_-m9HeaN3STbja0bINLsSbWzek-zftn5Em0fQnPT_OCXF9-_LX6zK6-f_qyWl4x10g-s7B22iJXAXVsIHTCN14rhbbVDfe2c1FGBC_Rc93qyCWgs-jXyltudfT8grw53t3m6W4XymyGVFzoezuGaVeMVNgp0ckKvv4PvJ12eay_GaWgE51GXiE8Qi5PpeQQzTanwea9QTAP_s3Rv6n-zYN_c6idl6fDu_UQ_N_GSXgFXh2BaCdjb3Iq5vpnA8gBtORCAf8DogqJmA</recordid><startdate>200405</startdate><enddate>200405</enddate><creator>Saigo, M</creator><creator>Bologna, F.P</creator><creator>Maurino, V.G</creator><creator>Detarsio, E</creator><creator>Andreo, C.S</creator><creator>Drincovich, M.F</creator><general>Springer Nature B.V</general><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>3V.</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200405</creationdate><title>Maize recombinant non-C4 NADP-malic enzyme: A novel dimeric malic enzyme with high specific activity</title><author>Saigo, M ; Bologna, F.P ; Maurino, V.G ; Detarsio, E ; Andreo, C.S ; Drincovich, M.F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c263t-ebc9a137e19f20e84d2d9771a5923da8cf6f10d61d3959f3601ca1db7da3a9fd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Blotting, Western</topic><topic>Cloning, Molecular</topic><topic>complementary DNA</topic><topic>Corn</topic><topic>Dimerization</topic><topic>DNA, Complementary - chemistry</topic><topic>DNA, Complementary - genetics</topic><topic>E coli</topic><topic>enzyme activity</topic><topic>Escherichia coli</topic><topic>gene expression</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Gene Expression Regulation, Plant</topic><topic>immunohistochemistry</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>isozymes</topic><topic>Kinetics</topic><topic>leaves</topic><topic>Malate Dehydrogenase - chemistry</topic><topic>Malate Dehydrogenase - genetics</topic><topic>Malate Dehydrogenase - metabolism</topic><topic>malic enzyme</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>nucleotide sequences</topic><topic>Photosynthesis</topic><topic>protein quaternary structure</topic><topic>recombinant proteins</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Roots</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>substrate specificity</topic><topic>Zea mays</topic><topic>Zea mays - enzymology</topic><topic>Zea mays - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saigo, M</creatorcontrib><creatorcontrib>Bologna, F.P</creatorcontrib><creatorcontrib>Maurino, V.G</creatorcontrib><creatorcontrib>Detarsio, E</creatorcontrib><creatorcontrib>Andreo, C.S</creatorcontrib><creatorcontrib>Drincovich, M.F</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Plant molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saigo, M</au><au>Bologna, F.P</au><au>Maurino, V.G</au><au>Detarsio, E</au><au>Andreo, C.S</au><au>Drincovich, M.F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Maize recombinant non-C4 NADP-malic enzyme: A novel dimeric malic enzyme with high specific activity</atitle><jtitle>Plant molecular biology</jtitle><addtitle>Plant Mol Biol</addtitle><date>2004-05</date><risdate>2004</risdate><volume>55</volume><issue>1</issue><spage>97</spage><epage>107</epage><pages>97-107</pages><issn>0167-4412</issn><eissn>1573-5028</eissn><abstract>Among the different isoforms of NADP-malic enzyme (NADP-ME) involved in a wide range of metabolic pathways in plants, the NADP-ME that participates in C4-photosynthesis is the most studied. In the present work, the expression in E. coli of a cDNA encoding for a maize non-photosynthetic NADP-ME is presented. The recombinant NADP-ME thus obtained presents kinetic and structural properties different from the enzyme previously purified from etiolated leaves and roots. Moreover, the recombinant non-photosynthetic NADP-ME presents very high intrinsic NADP-ME activity, which is unexpected for a non-C4 NADP-ME. Using antibodies against this recombinant enzyme, an immunoreactive band of 66 kDa is detected in different maize tissues indicating that the 66 kDa-NADP-ME is in fact a protein expressed in vivo. The recombinant NADP-ME assembles as a dimer, although the results obtained indicate that a higher molecular mass oligomeric state of the enzyme is found in maize roots in vivo. In this way, maize presents at least three NADP-ME isoforms: a 72 kDa constitutive form (previously characterized); the novel non-photosynthetic 66 kDa isoform characterized in this work (which is the product of the ZmChlMe2 gene and the likely precursor to the evolution of the photosynthetic C4 NADP-ME) and the 62 kDa isoform (implicated in C4 photosynthesis). The contribution of the present work anticipates further studies concerning the equilibrium between the oligomeric states of the NADP-ME isoforms and the evolution towards the C4 isoenzyme in maize.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>15604667</pmid><doi>10.1007/s11103-004-0472-z</doi><tpages>11</tpages></addata></record> |
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| ispartof | Plant molecular biology, 2004-05, Vol.55 (1), p.97-107 |
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| subjects | Amino Acid Sequence amino acid sequences Blotting, Western Cloning, Molecular complementary DNA Corn Dimerization DNA, Complementary - chemistry DNA, Complementary - genetics E coli enzyme activity Escherichia coli gene expression Gene Expression Regulation, Enzymologic Gene Expression Regulation, Plant immunohistochemistry Isoenzymes - chemistry Isoenzymes - genetics Isoenzymes - metabolism isozymes Kinetics leaves Malate Dehydrogenase - chemistry Malate Dehydrogenase - genetics Malate Dehydrogenase - metabolism malic enzyme Molecular Sequence Data Molecular Weight nucleotide sequences Photosynthesis protein quaternary structure recombinant proteins Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Reverse Transcriptase Polymerase Chain Reaction Roots Sequence Alignment Sequence Analysis, DNA Sequence Homology, Amino Acid substrate specificity Zea mays Zea mays - enzymology Zea mays - genetics |
| title | Maize recombinant non-C4 NADP-malic enzyme: A novel dimeric malic enzyme with high specific activity |
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