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Cloning and characterization of two maize cDNAs encoding Cinnamoyl-CoA Reductase (CCR) and differential expression of the corresponding genes
Cinnamoyl-CoA Reductase (CCR, EC 1.2.1.44) catalyses the first step of the lignin pathway. Two full-length cDNAs identified by sequence analysis as CCR-encoding cDNAs were isolated from a maize root cDNA library. These two cDNAs designated ZmCCR1 and ZmCCR2 exhibit 73% sequence conservation at the n...
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Published in: | Plant molecular biology 1998-11, Vol.38 (4), p.671-676 |
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container_title | Plant molecular biology |
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description | Cinnamoyl-CoA Reductase (CCR, EC 1.2.1.44) catalyses the first step of the lignin pathway. Two full-length cDNAs identified by sequence analysis as CCR-encoding cDNAs were isolated from a maize root cDNA library. These two cDNAs designated ZmCCR1 and ZmCCR2 exhibit 73% sequence conservation at the nucleotide level for their coding regions and are relatively divergent at their 5'- and 3'-untranslated regions. They both contain a common signature which is thought to be involved in the catalytic site of CCR. Northern blot analysis indicated that ZmCCR2 was expressed at very low levels in roots whereas ZmCCR1 was widely expressed in different organs. The high level of ZmCCR1 gene expression along the stalk suggests that the corresponding enzyme is probably involved in constitutive lignification. |
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(Station d'Amelioration des Plantes INRA, Clermont-Ferrand (France).) ; Courbou, I ; Beckert, M ; Boudet, A.M ; Grima-Pettenati, J</creator><creatorcontrib>Pichon, M. (Station d'Amelioration des Plantes INRA, Clermont-Ferrand (France).) ; Courbou, I ; Beckert, M ; Boudet, A.M ; Grima-Pettenati, J</creatorcontrib><description>Cinnamoyl-CoA Reductase (CCR, EC 1.2.1.44) catalyses the first step of the lignin pathway. Two full-length cDNAs identified by sequence analysis as CCR-encoding cDNAs were isolated from a maize root cDNA library. These two cDNAs designated ZmCCR1 and ZmCCR2 exhibit 73% sequence conservation at the nucleotide level for their coding regions and are relatively divergent at their 5'- and 3'-untranslated regions. They both contain a common signature which is thought to be involved in the catalytic site of CCR. Northern blot analysis indicated that ZmCCR2 was expressed at very low levels in roots whereas ZmCCR1 was widely expressed in different organs. The high level of ZmCCR1 gene expression along the stalk suggests that the corresponding enzyme is probably involved in constitutive lignification.</description><identifier>ISSN: 0167-4412</identifier><identifier>EISSN: 1573-5028</identifier><identifier>DOI: 10.1023/A:1006060101866</identifier><identifier>PMID: 9747812</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Aldehyde Oxidoreductases - genetics ; Amino Acid Sequence ; Binding Sites - genetics ; Cloning ; Cloning, Molecular ; Conserved Sequence ; Corn ; DNA ; DNA, Complementary - genetics ; DNA, Plant - genetics ; GENE EXPRESSION ; Genes, Plant ; Life Sciences ; Lignin - biosynthesis ; LIGNINS ; Molecular Sequence Data ; NUCLEOTIDE SEQUENCE ; PLANT ANATOMY ; Proteins ; Restriction Mapping ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNA, Plant - genetics ; RNA, Plant - metabolism ; ROOTS ; Sequence Homology, Amino Acid ; Vegetal Biology ; ZEA MAYS ; Zea mays - enzymology ; Zea mays - genetics</subject><ispartof>Plant molecular biology, 1998-11, Vol.38 (4), p.671-676</ispartof><rights>Kluwer Academic Publishers 1998</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-9b296815a9a0511a10d217cbd1dd047ca37e1f18d7c8bd944d5fb2fff1f1e6c73</citedby><orcidid>0000-0003-4272-9767</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9747812$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02699175$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Pichon, M. (Station d'Amelioration des Plantes INRA, Clermont-Ferrand (France).)</creatorcontrib><creatorcontrib>Courbou, I</creatorcontrib><creatorcontrib>Beckert, M</creatorcontrib><creatorcontrib>Boudet, A.M</creatorcontrib><creatorcontrib>Grima-Pettenati, J</creatorcontrib><title>Cloning and characterization of two maize cDNAs encoding Cinnamoyl-CoA Reductase (CCR) and differential expression of the corresponding genes</title><title>Plant molecular biology</title><addtitle>Plant Mol Biol</addtitle><description>Cinnamoyl-CoA Reductase (CCR, EC 1.2.1.44) catalyses the first step of the lignin pathway. Two full-length cDNAs identified by sequence analysis as CCR-encoding cDNAs were isolated from a maize root cDNA library. These two cDNAs designated ZmCCR1 and ZmCCR2 exhibit 73% sequence conservation at the nucleotide level for their coding regions and are relatively divergent at their 5'- and 3'-untranslated regions. They both contain a common signature which is thought to be involved in the catalytic site of CCR. Northern blot analysis indicated that ZmCCR2 was expressed at very low levels in roots whereas ZmCCR1 was widely expressed in different organs. The high level of ZmCCR1 gene expression along the stalk suggests that the corresponding enzyme is probably involved in constitutive lignification.</description><subject>Aldehyde Oxidoreductases - genetics</subject><subject>Amino Acid Sequence</subject><subject>Binding Sites - genetics</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Conserved Sequence</subject><subject>Corn</subject><subject>DNA</subject><subject>DNA, Complementary - genetics</subject><subject>DNA, Plant - genetics</subject><subject>GENE EXPRESSION</subject><subject>Genes, Plant</subject><subject>Life Sciences</subject><subject>Lignin - biosynthesis</subject><subject>LIGNINS</subject><subject>Molecular Sequence Data</subject><subject>NUCLEOTIDE SEQUENCE</subject><subject>PLANT ANATOMY</subject><subject>Proteins</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA, Plant - genetics</subject><subject>RNA, Plant - metabolism</subject><subject>ROOTS</subject><subject>Sequence Homology, Amino Acid</subject><subject>Vegetal Biology</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>1998</creationdate><recordtype>article</recordtype><recordid>eNqFkk1v1DAQhi0EKkvhzAnJ4oDoIeCJEzvmFgVKK62KVME5cvyx6yqxFztpaf8D_7luu4DUC_LB0juPH81ojNBrIB-AlPRj-wkIYfkAgYaxJ2gFNadFTcrmKVoRYLyoKiifoxcpXZBMEcoO0IHgFW-gXKHf3Ri88xssvcZqK6NUs4nuRs4ueBwsnq8CnqS7MVh9PmsTNl4Fffegc97LKVyPRRdafG70omaZDH7fdedH9zrtrDXR-NnJEZtfu2hS-mPdZl-IOdkFf6_bGG_SS_TMyjGZV_v7EP04_vK9OynW376edu26UHmWuRBDKVgDtRSS1AASiC6Bq0GD1qTiSlJuwEKjuWoGLapK13YorbU5NExxeoiOHrxbOfa76CYZr_sgXX_Srvu7jJRMCOD1JWT23QO7i-HnYtLcTy4pM47Sm7CknlNBgTH2XxBYJWra0Ay-fQRehCX6PHDPGRc1VLXI0Js9tAyT0X-73G_uX93K0MtNdKk_W4MQTf4OlWD0FqvRoy8</recordid><startdate>19981101</startdate><enddate>19981101</enddate><creator>Pichon, M. (Station d'Amelioration des Plantes INRA, Clermont-Ferrand (France).)</creator><creator>Courbou, I</creator><creator>Beckert, M</creator><creator>Boudet, A.M</creator><creator>Grima-Pettenati, J</creator><general>Springer Nature B.V</general><general>Springer Verlag (Germany)</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</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>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-4272-9767</orcidid></search><sort><creationdate>19981101</creationdate><title>Cloning and characterization of two maize cDNAs encoding Cinnamoyl-CoA Reductase (CCR) and differential expression of the corresponding genes</title><author>Pichon, M. (Station d'Amelioration des Plantes INRA, Clermont-Ferrand (France).) ; Courbou, I ; Beckert, M ; Boudet, A.M ; Grima-Pettenati, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-9b296815a9a0511a10d217cbd1dd047ca37e1f18d7c8bd944d5fb2fff1f1e6c73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Aldehyde Oxidoreductases - genetics</topic><topic>Amino Acid Sequence</topic><topic>Binding Sites - genetics</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>Conserved Sequence</topic><topic>Corn</topic><topic>DNA</topic><topic>DNA, Complementary - genetics</topic><topic>DNA, Plant - genetics</topic><topic>GENE EXPRESSION</topic><topic>Genes, Plant</topic><topic>Life Sciences</topic><topic>Lignin - biosynthesis</topic><topic>LIGNINS</topic><topic>Molecular Sequence Data</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>PLANT ANATOMY</topic><topic>Proteins</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA, Plant - genetics</topic><topic>RNA, Plant - metabolism</topic><topic>ROOTS</topic><topic>Sequence Homology, Amino Acid</topic><topic>Vegetal Biology</topic><topic>ZEA MAYS</topic><topic>Zea mays - enzymology</topic><topic>Zea mays - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pichon, M. (Station d'Amelioration des Plantes INRA, Clermont-Ferrand (France).)</creatorcontrib><creatorcontrib>Courbou, I</creatorcontrib><creatorcontrib>Beckert, M</creatorcontrib><creatorcontrib>Boudet, A.M</creatorcontrib><creatorcontrib>Grima-Pettenati, J</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest_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)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</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>PML(ProQuest Medical Library)</collection><collection>ProQuest_Research Library</collection><collection>ProQuest Biological Science Journals</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 Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Plant molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pichon, M. (Station d'Amelioration des Plantes INRA, Clermont-Ferrand (France).)</au><au>Courbou, I</au><au>Beckert, M</au><au>Boudet, A.M</au><au>Grima-Pettenati, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and characterization of two maize cDNAs encoding Cinnamoyl-CoA Reductase (CCR) and differential expression of the corresponding genes</atitle><jtitle>Plant molecular biology</jtitle><addtitle>Plant Mol Biol</addtitle><date>1998-11-01</date><risdate>1998</risdate><volume>38</volume><issue>4</issue><spage>671</spage><epage>676</epage><pages>671-676</pages><issn>0167-4412</issn><eissn>1573-5028</eissn><abstract>Cinnamoyl-CoA Reductase (CCR, EC 1.2.1.44) catalyses the first step of the lignin pathway. Two full-length cDNAs identified by sequence analysis as CCR-encoding cDNAs were isolated from a maize root cDNA library. These two cDNAs designated ZmCCR1 and ZmCCR2 exhibit 73% sequence conservation at the nucleotide level for their coding regions and are relatively divergent at their 5'- and 3'-untranslated regions. They both contain a common signature which is thought to be involved in the catalytic site of CCR. Northern blot analysis indicated that ZmCCR2 was expressed at very low levels in roots whereas ZmCCR1 was widely expressed in different organs. The high level of ZmCCR1 gene expression along the stalk suggests that the corresponding enzyme is probably involved in constitutive lignification.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>9747812</pmid><doi>10.1023/A:1006060101866</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0003-4272-9767</orcidid></addata></record> |
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subjects | Aldehyde Oxidoreductases - genetics Amino Acid Sequence Binding Sites - genetics Cloning Cloning, Molecular Conserved Sequence Corn DNA DNA, Complementary - genetics DNA, Plant - genetics GENE EXPRESSION Genes, Plant Life Sciences Lignin - biosynthesis LIGNINS Molecular Sequence Data NUCLEOTIDE SEQUENCE PLANT ANATOMY Proteins Restriction Mapping RNA, Messenger - genetics RNA, Messenger - metabolism RNA, Plant - genetics RNA, Plant - metabolism ROOTS Sequence Homology, Amino Acid Vegetal Biology ZEA MAYS Zea mays - enzymology Zea mays - genetics |
title | Cloning and characterization of two maize cDNAs encoding Cinnamoyl-CoA Reductase (CCR) and differential expression of the corresponding genes |
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