cDNA cloning, sequence analysis and seasonal expression of lignin-bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase of aspen.
Identifieur interne : 004C30 ( Main/Exploration ); précédent : 004C29; suivant : 004C31cDNA cloning, sequence analysis and seasonal expression of lignin-bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase of aspen.
Auteurs : R C Bugos ; V L Chiang ; W H CampbellSource :
- Plant molecular biology [ 0167-4412 ] ; 1991.
Descripteurs français
- KwdFr :
- ADN (MeSH), Acides caféiques (métabolisme), Acides coumariques (métabolisme), Animaux (MeSH), Arbres (MeSH), Banque génomique (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Lignine (métabolisme), Protein O-methyltransferase (génétique), Protein O-methyltransferase (métabolisme), Saisons (MeSH), Similitude de séquences d'acides nucléiques (MeSH), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Technique de Southern (MeSH).
- MESH :
- génétique : Protein O-methyltransferase.
- métabolisme : Acides caféiques, Acides coumariques, Lignine, Protein O-methyltransferase.
- ADN, Animaux, Arbres, Banque génomique, Clonage moléculaire, Données de séquences moléculaires, Saisons, Similitude de séquences d'acides nucléiques, Spécificité du substrat, Séquence d'acides aminés, Séquence nucléotidique, Technique de Southern.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Base Sequence (MeSH), Blotting, Southern (MeSH), Caffeic Acids (metabolism), Cloning, Molecular (MeSH), Coumaric Acids (metabolism), DNA (MeSH), Genomic Library (MeSH), Lignin (metabolism), Molecular Sequence Data (MeSH), Protein O-Methyltransferase (genetics), Protein O-Methyltransferase (metabolism), Seasons (MeSH), Sequence Homology, Nucleic Acid (MeSH), Substrate Specificity (MeSH), Trees (MeSH).
- MESH :
- chemical , genetics : Protein O-Methyltransferase.
- chemical , metabolism : Caffeic Acids, Coumaric Acids, Lignin, Protein O-Methyltransferase.
- Amino Acid Sequence, Animals, Base Sequence, Blotting, Southern, Cloning, Molecular, DNA, Genomic Library, Molecular Sequence Data, Seasons, Sequence Homology, Nucleic Acid, Substrate Specificity, Trees.
Abstract
A cDNA clone (Ptomt 1) encoding a lignin-bispecific O-methyltransferase (OMT) was isolated by immunological screening of a lambda gt11 expression library prepared from mRNA of developing secondary xylem of aspen (Populus tremuloides). Nucleotide sequence analysis of Ptomt1 revealed an open reading frame of 1095 bp which encodes a polypeptide with a predicted molecular weight of 39,802, corresponding well with the size of the OMT polypeptide estimated by SDS-PAGE. Authenticity of Ptomt1 was demonstrated in part by detection of OMT activity and protein in extracts of Escherichia coli cultures transformed with a plasmid construct containing Ptomt1. In addition, peptides produced from a proteolytic digest of purified OMT and sequenced by automated Edman degradation matched to portions of the deduced amino acid sequence of Ptomt1. Comparison of this sequence to amino acid sequences of OMTs of diverse species identified regions of similarity which probably contribute to the binding site of S-adenosyl-L-methionine. Tissue-specific expression was demonstrated by northern analysis which showed that Ptomt1 hybridized to a 1.7 kb transcript from aspen developing secondary xylem and by tissue printing of aspen stems in which only the outer layer of xylem bound the antibody. A biphasic pattern of gene expression and enzyme activity for OMT was observed from xylem samples of aspen during the growing season which suggests linkage between gene expression for a monolignol biosynthetic enzyme and seasonal regulation of xylem differentiation in woody plants.
DOI: 10.1007/BF00028736
PubMed: 1932694
Affiliations:
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uniqKey="Chiang V" first="V L" last="Chiang">V L Chiang</name></author><author><name sortKey="Campbell, W H" sort="Campbell, W H" uniqKey="Campbell W" first="W H" last="Campbell">W H Campbell</name></author></analytic><series><title level="j">Plant molecular biology</title><idno type="ISSN">0167-4412</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Base Sequence (MeSH)</term><term>Blotting, Southern (MeSH)</term><term>Caffeic Acids (metabolism)</term><term>Cloning, Molecular (MeSH)</term><term>Coumaric Acids (metabolism)</term><term>DNA (MeSH)</term><term>Genomic Library (MeSH)</term><term>Lignin (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Protein O-Methyltransferase (genetics)</term><term>Protein O-Methyltransferase (metabolism)</term><term>Seasons (MeSH)</term><term>Sequence Homology, Nucleic Acid (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Trees (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN (MeSH)</term><term>Acides caféiques (métabolisme)</term><term>Acides coumariques (métabolisme)</term><term>Animaux (MeSH)</term><term>Arbres (MeSH)</term><term>Banque génomique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Lignine (métabolisme)</term><term>Protein O-methyltransferase (génétique)</term><term>Protein O-methyltransferase (métabolisme)</term><term>Saisons (MeSH)</term><term>Similitude de séquences d'acides nucléiques (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Technique de Southern (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Protein O-Methyltransferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Caffeic Acids</term><term>Coumaric Acids</term><term>Lignin</term><term>Protein O-Methyltransferase</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protein O-methyltransferase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides caféiques</term><term>Acides coumariques</term><term>Lignine</term><term>Protein O-methyltransferase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Blotting, Southern</term><term>Cloning, Molecular</term><term>DNA</term><term>Genomic Library</term><term>Molecular Sequence Data</term><term>Seasons</term><term>Sequence Homology, Nucleic Acid</term><term>Substrate Specificity</term><term>Trees</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN</term><term>Animaux</term><term>Arbres</term><term>Banque génomique</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Saisons</term><term>Similitude de séquences d'acides nucléiques</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Technique de Southern</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A cDNA clone (Ptomt 1) encoding a lignin-bispecific O-methyltransferase (OMT) was isolated by immunological screening of a lambda gt11 expression library prepared from mRNA of developing secondary xylem of aspen (Populus tremuloides). Nucleotide sequence analysis of Ptomt1 revealed an open reading frame of 1095 bp which encodes a polypeptide with a predicted molecular weight of 39,802, corresponding well with the size of the OMT polypeptide estimated by SDS-PAGE. Authenticity of Ptomt1 was demonstrated in part by detection of OMT activity and protein in extracts of Escherichia coli cultures transformed with a plasmid construct containing Ptomt1. In addition, peptides produced from a proteolytic digest of purified OMT and sequenced by automated Edman degradation matched to portions of the deduced amino acid sequence of Ptomt1. Comparison of this sequence to amino acid sequences of OMTs of diverse species identified regions of similarity which probably contribute to the binding site of S-adenosyl-L-methionine. Tissue-specific expression was demonstrated by northern analysis which showed that Ptomt1 hybridized to a 1.7 kb transcript from aspen developing secondary xylem and by tissue printing of aspen stems in which only the outer layer of xylem bound the antibody. A biphasic pattern of gene expression and enzyme activity for OMT was observed from xylem samples of aspen during the growing season which suggests linkage between gene expression for a monolignol biosynthetic enzyme and seasonal regulation of xylem differentiation in woody plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1932694</PMID><DateCompleted><Year>1991</Year><Month>12</Month><Day>24</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0167-4412</ISSN><JournalIssue CitedMedium="Print"><Volume>17</Volume><Issue>6</Issue><PubDate><Year>1991</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Plant molecular biology</Title><ISOAbbreviation>Plant Mol Biol</ISOAbbreviation></Journal><ArticleTitle>cDNA cloning, sequence analysis and seasonal expression of lignin-bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase of aspen.</ArticleTitle><Pagination><MedlinePgn>1203-15</MedlinePgn></Pagination><Abstract><AbstractText>A cDNA clone (Ptomt 1) encoding a lignin-bispecific O-methyltransferase (OMT) was isolated by immunological screening of a lambda gt11 expression library prepared from mRNA of developing secondary xylem of aspen (Populus tremuloides). Nucleotide sequence analysis of Ptomt1 revealed an open reading frame of 1095 bp which encodes a polypeptide with a predicted molecular weight of 39,802, corresponding well with the size of the OMT polypeptide estimated by SDS-PAGE. Authenticity of Ptomt1 was demonstrated in part by detection of OMT activity and protein in extracts of Escherichia coli cultures transformed with a plasmid construct containing Ptomt1. In addition, peptides produced from a proteolytic digest of purified OMT and sequenced by automated Edman degradation matched to portions of the deduced amino acid sequence of Ptomt1. Comparison of this sequence to amino acid sequences of OMTs of diverse species identified regions of similarity which probably contribute to the binding site of S-adenosyl-L-methionine. Tissue-specific expression was demonstrated by northern analysis which showed that Ptomt1 hybridized to a 1.7 kb transcript from aspen developing secondary xylem and by tissue printing of aspen stems in which only the outer layer of xylem bound the antibody. A biphasic pattern of gene expression and enzyme activity for OMT was observed from xylem samples of aspen during the growing season which suggests linkage between gene expression for a monolignol biosynthetic enzyme and seasonal regulation of xylem differentiation in woody plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bugos</LastName><ForeName>R C</ForeName><Initials>RC</Initials><AffiliationInfo><Affiliation>Phytotechnology Research Center, Michigan Technological University, Houghton 49931.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chiang</LastName><ForeName>V L</ForeName><Initials>VL</Initials></Author><Author ValidYN="Y"><LastName>Campbell</LastName><ForeName>W H</ForeName><Initials>WH</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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IdType="pubmed">2849754</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Bugos, R C" sort="Bugos, R C" uniqKey="Bugos R" first="R C" last="Bugos">R C Bugos</name><name sortKey="Campbell, W H" sort="Campbell, W H" uniqKey="Campbell W" first="W H" last="Campbell">W H Campbell</name><name sortKey="Chiang, V L" sort="Chiang, V L" uniqKey="Chiang V" first="V L" last="Chiang">V L Chiang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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