Molecular cloning and biochemical characterization of indole-3-acetic acid methyltransferase from poplar.
Identifieur interne : 003B18 ( Main/Exploration ); précédent : 003B17; suivant : 003B19Molecular cloning and biochemical characterization of indole-3-acetic acid methyltransferase from poplar.
Auteurs : Nan Zhao [États-Unis] ; Ju Guan ; Hong Lin ; Feng ChenSource :
- Phytochemistry [ 0031-9422 ] ; 2007.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Cinétique (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Methyltransferases (composition chimique), Methyltransferases (génétique), Methyltransferases (physiologie), Phylogenèse (MeSH), Populus (enzymologie), Populus (génétique), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (physiologie), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Methyltransferases, Protéines recombinantes, Protéines végétales.
- enzymologie : Populus.
- génétique : Methyltransferases, Populus, Protéines recombinantes, Protéines végétales.
- métabolisme : Protéines recombinantes.
- physiologie : Methyltransferases, Protéines végétales.
- Alignement de séquences, Cinétique, Clonage moléculaire, Données de séquences moléculaires, Phylogenèse, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Cloning, Molecular (MeSH), Kinetics (MeSH), Methyltransferases (chemistry), Methyltransferases (genetics), Methyltransferases (physiology), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (physiology), Populus (enzymology), Populus (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Methyltransferases, Plant Proteins, Recombinant Proteins.
- chemical , genetics : Methyltransferases, Plant Proteins, Recombinant Proteins.
- chemical , metabolism : Recombinant Proteins.
- chemical , physiology : Methyltransferases, Plant Proteins.
- enzymology : Populus.
- genetics : Populus.
- Amino Acid Sequence, Cloning, Molecular, Kinetics, Molecular Sequence Data, Phylogeny, Sequence Alignment, Substrate Specificity.
Abstract
Indole-3-acetic acid (IAA) is the most active endogenous auxin and is involved in various physiological processes in higher plants. Concentrations of IAA in plant tissues are regulated at multiple levels including de novo biosynthesis, conjugation/deconjugation, and degradation. In this paper, we report molecular isolation and biochemical characterization of a gene PtIAMT1 from poplar encoding IAA methyltransferase (IAMT), which plays a role in regulating IAA homeostasis. PtIAMT1 was identified from the poplar genome based on sequence similarity to Arabidopsis IAMT. A full-length cDNA of PtIAMT1 was cloned from poplar roots via RT-PCR. Recombinant PtIAMT1 expressed in Escherichia coli was purified to electrophoretic homogeneity. Enzyme assays combined with GC-MS verified that PtIAMT1 catalyzes formation of methyl indole-3-acetate using S-adenosyl-l-methionine (SAM) as a methyl donor and IAA as a methyl acceptor. PtIAMT1 had a temperature optimum at 25 degrees C and a pH optimum at pH 7.5. Its activity was promoted by K(+) but inhibited by Fe(2+), Cu(2+) and Zn(2+). Under steady-state conditions, PtIAMT1 exhibited apparent K(m) values of 23.1 microM and 30.4 microM for IAA and SAM, respectively. Gene expression analysis showed that PtIAMT1 had the highest level of expression in stems, a moderate level of expression in young leaves, and a low level of expression in roots. Presence of PtIAMT1 transcripts in several organs suggests that PtIAMT1 is involved in development of multiple organs in poplar.
DOI: 10.1016/j.phytochem.2007.03.041
PubMed: 17499822
Affiliations:
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last="Lin">Hong Lin</name></author><author><name sortKey="Chen, Feng" sort="Chen, Feng" uniqKey="Chen F" first="Feng" last="Chen">Feng Chen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17499822</idno><idno type="pmid">17499822</idno><idno type="doi">10.1016/j.phytochem.2007.03.041</idno><idno type="wicri:Area/Main/Corpus">003B55</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003B55</idno><idno type="wicri:Area/Main/Curation">003B55</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003B55</idno><idno type="wicri:Area/Main/Exploration">003B55</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular cloning and biochemical characterization of indole-3-acetic acid methyltransferase from poplar.</title><author><name sortKey="Zhao, Nan" sort="Zhao, Nan" uniqKey="Zhao N" first="Nan" last="Zhao">Nan Zhao</name><affiliation wicri:level="2"><nlm:affiliation>Department of Plant Sciences, 252 Ellington Plant Sciences Building, University of Tennessee, 2431 Joe Johnson Drive, Knoxville, TN 37996, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Plant Sciences, 252 Ellington Plant Sciences Building, University of Tennessee, 2431 Joe Johnson Drive, Knoxville, TN 37996</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author><author><name sortKey="Guan, Ju" sort="Guan, Ju" uniqKey="Guan J" first="Ju" last="Guan">Ju Guan</name></author><author><name sortKey="Lin, Hong" sort="Lin, Hong" uniqKey="Lin H" first="Hong" last="Lin">Hong Lin</name></author><author><name sortKey="Chen, Feng" sort="Chen, Feng" uniqKey="Chen F" first="Feng" last="Chen">Feng Chen</name></author></analytic><series><title level="j">Phytochemistry</title><idno type="ISSN">0031-9422</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Kinetics (MeSH)</term><term>Methyltransferases (chemistry)</term><term>Methyltransferases (genetics)</term><term>Methyltransferases (physiology)</term><term>Molecular Sequence Data (MeSH)</term><term>Phylogeny (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (physiology)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Methyltransferases (composition chimique)</term><term>Methyltransferases (génétique)</term><term>Methyltransferases (physiologie)</term><term>Phylogenèse (MeSH)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (physiologie)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Methyltransferases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Methyltransferases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Methyltransferases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Methyltransferases</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Methyltransferases</term><term>Populus</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Methyltransferases</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Sequence Alignment</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Cinétique</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Phylogenèse</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Indole-3-acetic acid (IAA) is the most active endogenous auxin and is involved in various physiological processes in higher plants. Concentrations of IAA in plant tissues are regulated at multiple levels including de novo biosynthesis, conjugation/deconjugation, and degradation. In this paper, we report molecular isolation and biochemical characterization of a gene PtIAMT1 from poplar encoding IAA methyltransferase (IAMT), which plays a role in regulating IAA homeostasis. PtIAMT1 was identified from the poplar genome based on sequence similarity to Arabidopsis IAMT. A full-length cDNA of PtIAMT1 was cloned from poplar roots via RT-PCR. Recombinant PtIAMT1 expressed in Escherichia coli was purified to electrophoretic homogeneity. Enzyme assays combined with GC-MS verified that PtIAMT1 catalyzes formation of methyl indole-3-acetate using S-adenosyl-l-methionine (SAM) as a methyl donor and IAA as a methyl acceptor. PtIAMT1 had a temperature optimum at 25 degrees C and a pH optimum at pH 7.5. Its activity was promoted by K(+) but inhibited by Fe(2+), Cu(2+) and Zn(2+). Under steady-state conditions, PtIAMT1 exhibited apparent K(m) values of 23.1 microM and 30.4 microM for IAA and SAM, respectively. Gene expression analysis showed that PtIAMT1 had the highest level of expression in stems, a moderate level of expression in young leaves, and a low level of expression in roots. Presence of PtIAMT1 transcripts in several organs suggests that PtIAMT1 is involved in development of multiple organs in poplar.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17499822</PMID><DateCompleted><Year>2007</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2007</Year><Month>05</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0031-9422</ISSN><JournalIssue CitedMedium="Print"><Volume>68</Volume><Issue>11</Issue><PubDate><Year>2007</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Phytochemistry</Title><ISOAbbreviation>Phytochemistry</ISOAbbreviation></Journal><ArticleTitle>Molecular cloning and biochemical characterization of indole-3-acetic acid methyltransferase from poplar.</ArticleTitle><Pagination><MedlinePgn>1537-44</MedlinePgn></Pagination><Abstract><AbstractText>Indole-3-acetic acid (IAA) is the most active endogenous auxin and is involved in various physiological processes in higher plants. Concentrations of IAA in plant tissues are regulated at multiple levels including de novo biosynthesis, conjugation/deconjugation, and degradation. In this paper, we report molecular isolation and biochemical characterization of a gene PtIAMT1 from poplar encoding IAA methyltransferase (IAMT), which plays a role in regulating IAA homeostasis. PtIAMT1 was identified from the poplar genome based on sequence similarity to Arabidopsis IAMT. A full-length cDNA of PtIAMT1 was cloned from poplar roots via RT-PCR. Recombinant PtIAMT1 expressed in Escherichia coli was purified to electrophoretic homogeneity. Enzyme assays combined with GC-MS verified that PtIAMT1 catalyzes formation of methyl indole-3-acetate using S-adenosyl-l-methionine (SAM) as a methyl donor and IAA as a methyl acceptor. PtIAMT1 had a temperature optimum at 25 degrees C and a pH optimum at pH 7.5. Its activity was promoted by K(+) but inhibited by Fe(2+), Cu(2+) and Zn(2+). Under steady-state conditions, PtIAMT1 exhibited apparent K(m) values of 23.1 microM and 30.4 microM for IAA and SAM, respectively. Gene expression analysis showed that PtIAMT1 had the highest level of expression in stems, a moderate level of expression in young leaves, and a low level of expression in roots. Presence of PtIAMT1 transcripts in several organs suggests that PtIAMT1 is involved in development of multiple organs in poplar.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Nan</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Plant Sciences, 252 Ellington Plant Sciences Building, University of Tennessee, 2431 Joe Johnson Drive, Knoxville, TN 37996, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guan</LastName><ForeName>Ju</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Hong</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Feng</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>05</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Phytochemistry</MedlineTA><NlmUniqueID>0151434</NlmUniqueID><ISSNLinking>0031-9422</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>07</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>03</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>03</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>5</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>9</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>5</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17499822</ArticleId><ArticleId IdType="pii">S0031-9422(07)00213-0</ArticleId><ArticleId IdType="doi">10.1016/j.phytochem.2007.03.041</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Tennessee</li></region></list><tree><noCountry><name sortKey="Chen, Feng" sort="Chen, Feng" uniqKey="Chen F" first="Feng" last="Chen">Feng Chen</name><name sortKey="Guan, Ju" sort="Guan, Ju" uniqKey="Guan J" first="Ju" last="Guan">Ju Guan</name><name sortKey="Lin, Hong" sort="Lin, Hong" uniqKey="Lin H" first="Hong" last="Lin">Hong Lin</name></noCountry><country name="États-Unis"><region name="Tennessee"><name sortKey="Zhao, Nan" sort="Zhao, Nan" uniqKey="Zhao N" first="Nan" last="Zhao">Nan Zhao</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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