Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells

We have isolated, cloned, and characterized two cDNAs corresponding to the mRNAs for cationic peroxidases synthesized by cultured peanut cells. The first clone was obtained from a phage γgt11 library screened with antibodies directed against the major secreted isozyme. Its predicted amino acid seque...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1990-11, Vol.87 (22), p.8874-8878
Hauptverfasser: Buffard, D. (Centre National de la Recherche Scientifique, Gif-sur-Yvette, France), Breda, C, Huystee, R.B. van, Asemota, O, Pierre, M, Dang Ha, D.B, Esnault, R
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creator Buffard, D. (Centre National de la Recherche Scientifique, Gif-sur-Yvette, France)
Breda, C
Huystee, R.B. van
Asemota, O
Pierre, M
Dang Ha, D.B
Esnault, R
description We have isolated, cloned, and characterized two cDNAs corresponding to the mRNAs for cationic peroxidases synthesized by cultured peanut cells. The first clone was obtained from a phage γgt11 library screened with antibodies directed against the major secreted isozyme. Its predicted amino acid sequence, deduced from the 1228-base-pair (bp) cDNA, revealed a 22-amino acid signal peptide and a 294-amino acid mature protein (Mr, 31,228). The second clone was isolated from a γgt10 library screened with oligonucleotides corresponding to the regions for acid/base catalysis and the fifth ligand of heme. This cDNA (1344 bp) encodes a protein (330 amino acids) with a mature peptide of 307 residues (Mr,32,954). The two peanut peroxidases are 46% homologous. The estimated gene copy numbers of these peroxidases might be close to 1 or 2 per haploid genome. A comparison of the amino acid sequence of these peanut peroxidases with other known isozymes shows two already known regions of homology (the region for acid/base catalysis and the fifth ligand of heme). Moreover, some new characteristics appeared such as a glycosylation site identical in five of the seven isozymes, a putative antigenic determinant common to all the isozymes, and a region of the highest homology. A secondary structure prediction showed that it corresponds to a 16-amino acid helix linked to the next one by a long stretch of β strands and coils and might represent a critical structural element.
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(Centre National de la Recherche Scientifique, Gif-sur-Yvette, France) ; Breda, C ; Huystee, R.B. van ; Asemota, O ; Pierre, M ; Dang Ha, D.B ; Esnault, R</creator><creatorcontrib>Buffard, D. (Centre National de la Recherche Scientifique, Gif-sur-Yvette, France) ; Breda, C ; Huystee, R.B. van ; Asemota, O ; Pierre, M ; Dang Ha, D.B ; Esnault, R</creatorcontrib><description>We have isolated, cloned, and characterized two cDNAs corresponding to the mRNAs for cationic peroxidases synthesized by cultured peanut cells. The first clone was obtained from a phage γgt11 library screened with antibodies directed against the major secreted isozyme. Its predicted amino acid sequence, deduced from the 1228-base-pair (bp) cDNA, revealed a 22-amino acid signal peptide and a 294-amino acid mature protein (Mr, 31,228). The second clone was isolated from a γgt10 library screened with oligonucleotides corresponding to the regions for acid/base catalysis and the fifth ligand of heme. This cDNA (1344 bp) encodes a protein (330 amino acids) with a mature peptide of 307 residues (Mr,32,954). The two peanut peroxidases are 46% homologous. The estimated gene copy numbers of these peroxidases might be close to 1 or 2 per haploid genome. A comparison of the amino acid sequence of these peanut peroxidases with other known isozymes shows two already known regions of homology (the region for acid/base catalysis and the fifth ligand of heme). Moreover, some new characteristics appeared such as a glycosylation site identical in five of the seven isozymes, a putative antigenic determinant common to all the isozymes, and a region of the highest homology. A secondary structure prediction showed that it corresponds to a 16-amino acid helix linked to the next one by a long stretch of β strands and coils and might represent a critical structural element.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.87.22.8874</identifier><identifier>PMID: 2247460</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>ADN ; Amino Acid Sequence ; AMINO ACID SEQUENCES ; Amino acids ; Arachis - genetics ; ARACHIS HYPOGAEA ; Base Sequence ; Biological and medical sciences ; Blotting, Southern ; Cells, Cultured ; CLONACION ; CLONAGE ; CLONING ; Cloning, Molecular ; CODE GENETIQUE ; CODIGO GENETICO ; Complementary DNA ; Cultured cells ; DNA ; DNA - genetics ; embl/m37636 ; EXPRESION GENICA ; EXPRESSION DES GENES ; Fundamental and applied biological sciences. 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(Centre National de la Recherche Scientifique, Gif-sur-Yvette, France)</creatorcontrib><creatorcontrib>Breda, C</creatorcontrib><creatorcontrib>Huystee, R.B. van</creatorcontrib><creatorcontrib>Asemota, O</creatorcontrib><creatorcontrib>Pierre, M</creatorcontrib><creatorcontrib>Dang Ha, D.B</creatorcontrib><creatorcontrib>Esnault, R</creatorcontrib><title>Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We have isolated, cloned, and characterized two cDNAs corresponding to the mRNAs for cationic peroxidases synthesized by cultured peanut cells. The first clone was obtained from a phage γgt11 library screened with antibodies directed against the major secreted isozyme. Its predicted amino acid sequence, deduced from the 1228-base-pair (bp) cDNA, revealed a 22-amino acid signal peptide and a 294-amino acid mature protein (Mr, 31,228). The second clone was isolated from a γgt10 library screened with oligonucleotides corresponding to the regions for acid/base catalysis and the fifth ligand of heme. This cDNA (1344 bp) encodes a protein (330 amino acids) with a mature peptide of 307 residues (Mr,32,954). The two peanut peroxidases are 46% homologous. The estimated gene copy numbers of these peroxidases might be close to 1 or 2 per haploid genome. A comparison of the amino acid sequence of these peanut peroxidases with other known isozymes shows two already known regions of homology (the region for acid/base catalysis and the fifth ligand of heme). Moreover, some new characteristics appeared such as a glycosylation site identical in five of the seven isozymes, a putative antigenic determinant common to all the isozymes, and a region of the highest homology. A secondary structure prediction showed that it corresponds to a 16-amino acid helix linked to the next one by a long stretch of β strands and coils and might represent a critical structural element.</description><subject>ADN</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACID SEQUENCES</subject><subject>Amino acids</subject><subject>Arachis - genetics</subject><subject>ARACHIS HYPOGAEA</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Southern</subject><subject>Cells, Cultured</subject><subject>CLONACION</subject><subject>CLONAGE</subject><subject>CLONING</subject><subject>Cloning, Molecular</subject><subject>CODE GENETIQUE</subject><subject>CODIGO GENETICO</subject><subject>Complementary DNA</subject><subject>Cultured cells</subject><subject>DNA</subject><subject>DNA - genetics</subject><subject>embl/m37636</subject><subject>EXPRESION GENICA</subject><subject>EXPRESSION DES GENES</subject><subject>Fundamental and applied biological sciences. 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(Centre National de la Recherche Scientifique, Gif-sur-Yvette, France)</creator><creator>Breda, C</creator><creator>Huystee, R.B. van</creator><creator>Asemota, O</creator><creator>Pierre, M</creator><creator>Dang Ha, D.B</creator><creator>Esnault, R</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</scope><scope>IQODW</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>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19901101</creationdate><title>Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells</title><author>Buffard, D. (Centre National de la Recherche Scientifique, Gif-sur-Yvette, France) ; Breda, C ; Huystee, R.B. van ; Asemota, O ; Pierre, M ; Dang Ha, D.B ; Esnault, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4574-53d55dff47a0840cd5a4c63d7396d1b0f606797eb1d7b185f14186415943d2833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>ADN</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACID SEQUENCES</topic><topic>Amino acids</topic><topic>Arachis - genetics</topic><topic>ARACHIS HYPOGAEA</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Southern</topic><topic>Cells, Cultured</topic><topic>CLONACION</topic><topic>CLONAGE</topic><topic>CLONING</topic><topic>Cloning, Molecular</topic><topic>CODE GENETIQUE</topic><topic>CODIGO GENETICO</topic><topic>Complementary DNA</topic><topic>Cultured cells</topic><topic>DNA</topic><topic>DNA - genetics</topic><topic>embl/m37636</topic><topic>EXPRESION GENICA</topic><topic>EXPRESSION DES GENES</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genbank/m37637</topic><topic>GENE</topic><topic>GENE EXPRESSION</topic><topic>Gene Library</topic><topic>GENE MAPPING</topic><topic>GENES</topic><topic>GENETIC CODE</topic><topic>GENETICA MOLECULAR</topic><topic>GENETIQUE MOLECULAIRE</topic><topic>Horseradish</topic><topic>Libraries</topic><topic>Molecular and cellular biology</topic><topic>MOLECULAR GENETICS</topic><topic>Molecular Sequence Data</topic><topic>NUCLEOTIDE</topic><topic>NUCLEOTIDES</topic><topic>NUCLEOTIDOS</topic><topic>Oligonucleotide probes</topic><topic>Oligonucleotides</topic><topic>Peanuts</topic><topic>PEROXIDASAS</topic><topic>PEROXIDASES</topic><topic>Peroxidases - genetics</topic><topic>PEROXYDASE</topic><topic>Plant cells</topic><topic>Turnips</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Buffard, D. (Centre National de la Recherche Scientifique, Gif-sur-Yvette, France)</creatorcontrib><creatorcontrib>Breda, C</creatorcontrib><creatorcontrib>Huystee, R.B. van</creatorcontrib><creatorcontrib>Asemota, O</creatorcontrib><creatorcontrib>Pierre, M</creatorcontrib><creatorcontrib>Dang Ha, D.B</creatorcontrib><creatorcontrib>Esnault, R</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Buffard, D. (Centre National de la Recherche Scientifique, Gif-sur-Yvette, France)</au><au>Breda, C</au><au>Huystee, R.B. van</au><au>Asemota, O</au><au>Pierre, M</au><au>Dang Ha, D.B</au><au>Esnault, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1990-11-01</date><risdate>1990</risdate><volume>87</volume><issue>22</issue><spage>8874</spage><epage>8878</epage><pages>8874-8878</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>We have isolated, cloned, and characterized two cDNAs corresponding to the mRNAs for cationic peroxidases synthesized by cultured peanut cells. The first clone was obtained from a phage γgt11 library screened with antibodies directed against the major secreted isozyme. Its predicted amino acid sequence, deduced from the 1228-base-pair (bp) cDNA, revealed a 22-amino acid signal peptide and a 294-amino acid mature protein (Mr, 31,228). The second clone was isolated from a γgt10 library screened with oligonucleotides corresponding to the regions for acid/base catalysis and the fifth ligand of heme. This cDNA (1344 bp) encodes a protein (330 amino acids) with a mature peptide of 307 residues (Mr,32,954). The two peanut peroxidases are 46% homologous. The estimated gene copy numbers of these peroxidases might be close to 1 or 2 per haploid genome. A comparison of the amino acid sequence of these peanut peroxidases with other known isozymes shows two already known regions of homology (the region for acid/base catalysis and the fifth ligand of heme). Moreover, some new characteristics appeared such as a glycosylation site identical in five of the seven isozymes, a putative antigenic determinant common to all the isozymes, and a region of the highest homology. A secondary structure prediction showed that it corresponds to a 16-amino acid helix linked to the next one by a long stretch of β strands and coils and might represent a critical structural element.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2247460</pmid><doi>10.1073/pnas.87.22.8874</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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source Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry
subjects ADN
Amino Acid Sequence
AMINO ACID SEQUENCES
Amino acids
Arachis - genetics
ARACHIS HYPOGAEA
Base Sequence
Biological and medical sciences
Blotting, Southern
Cells, Cultured
CLONACION
CLONAGE
CLONING
Cloning, Molecular
CODE GENETIQUE
CODIGO GENETICO
Complementary DNA
Cultured cells
DNA
DNA - genetics
embl/m37636
EXPRESION GENICA
EXPRESSION DES GENES
Fundamental and applied biological sciences. Psychology
genbank/m37637
GENE
GENE EXPRESSION
Gene Library
GENE MAPPING
GENES
GENETIC CODE
GENETICA MOLECULAR
GENETIQUE MOLECULAIRE
Horseradish
Libraries
Molecular and cellular biology
MOLECULAR GENETICS
Molecular Sequence Data
NUCLEOTIDE
NUCLEOTIDES
NUCLEOTIDOS
Oligonucleotide probes
Oligonucleotides
Peanuts
PEROXIDASAS
PEROXIDASES
Peroxidases - genetics
PEROXYDASE
Plant cells
Turnips
title Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells
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