Isolation and Characterization of O-methyltransferases Involved in the Biosynthesis of Glaucine in Glaucium flavum1
Identifieur interne : 000007 ( Pmc/Corpus ); précédent : 000006; suivant : 000008Isolation and Characterization of O-methyltransferases Involved in the Biosynthesis of Glaucine in Glaucium flavum1
Auteurs : Limei Chang ; Jillian M. Hagel ; Peter J. FacchiniSource :
- Plant Physiology [ 0032-0889 ] ; 2015.
Abstract
A subset of multifunctional O-methyltransferases is involved in the formation of the tetra-O-methylated benzylisoquinoline alkaloid glaucine.
Url:
DOI: 10.1104/pp.15.01240
PubMed: 26297140
PubMed Central: 4587479
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PMC:4587479Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Isolation and Characterization of <italic>O</italic>-methyltransferases Involved in the Biosynthesis of Glaucine in <italic>Glaucium flavum</italic><xref ref-type="fn" rid="fn1"><sup>1</sup></xref></title><author><name sortKey="Chang, Limei" sort="Chang, Limei" uniqKey="Chang L" first="Limei" last="Chang">Limei Chang</name></author><author><name sortKey="Hagel, Jillian M" sort="Hagel, Jillian M" uniqKey="Hagel J" first="Jillian M." last="Hagel">Jillian M. Hagel</name></author><author><name sortKey="Facchini, Peter J" sort="Facchini, Peter J" uniqKey="Facchini P" first="Peter J." last="Facchini">Peter J. Facchini</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">26297140</idno><idno type="pmc">4587479</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4587479</idno><idno type="RBID">PMC:4587479</idno><idno type="doi">10.1104/pp.15.01240</idno><date when="2015">2015</date><idno type="wicri:Area/Pmc/Corpus">000007</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000007</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Isolation and Characterization of <italic>O</italic>-methyltransferases Involved in the Biosynthesis of Glaucine in <italic>Glaucium flavum</italic><xref ref-type="fn" rid="fn1"><sup>1</sup></xref></title><author><name sortKey="Chang, Limei" sort="Chang, Limei" uniqKey="Chang L" first="Limei" last="Chang">Limei Chang</name></author><author><name sortKey="Hagel, Jillian M" sort="Hagel, Jillian M" uniqKey="Hagel J" first="Jillian M." last="Hagel">Jillian M. Hagel</name></author><author><name sortKey="Facchini, Peter J" sort="Facchini, Peter J" uniqKey="Facchini P" first="Peter J." last="Facchini">Peter J. Facchini</name></author></analytic><series><title level="j">Plant Physiology</title><idno type="ISSN">0032-0889</idno><idno type="eISSN">1532-2548</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>A subset of multifunctional O-methyltransferases is involved in the formation of the tetra-O-methylated benzylisoquinoline alkaloid glaucine.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant Physiol</journal-id><journal-id journal-id-type="iso-abbrev">Plant Physiol</journal-id><journal-id journal-id-type="hwp">plantphysiol</journal-id><journal-id journal-id-type="publisher-id">aspb</journal-id><journal-title-group><journal-title>Plant Physiology</journal-title></journal-title-group><issn pub-type="ppub">0032-0889</issn><issn pub-type="epub">1532-2548</issn><publisher><publisher-name>American Society of Plant Biologists</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">26297140</article-id><article-id pub-id-type="pmc">4587479</article-id><article-id pub-id-type="publisher-id">PP201501240</article-id><article-id pub-id-type="doi">10.1104/pp.15.01240</article-id><article-categories><subj-group subj-group-type="heading"><subject>Articles</subject><subj-group subj-group-type="heading"><subject>Biochemistry and Metabolism</subject></subj-group></subj-group></article-categories><title-group><article-title>Isolation and Characterization of <italic>O</italic>-methyltransferases Involved in the Biosynthesis of Glaucine in <italic>Glaucium flavum</italic><xref ref-type="fn" rid="fn1"><sup>1</sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Chang</surname><given-names>Limei</given-names></name></contrib><contrib contrib-type="author"><name><surname>Hagel</surname><given-names>Jillian M.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Facchini</surname><given-names>Peter J.</given-names></name><xref ref-type="corresp" rid="cor1">*</xref></contrib><aff id="aff1">Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada</aff></contrib-group><author-notes><fn><p><ext-link ext-link-type="uri" xlink:href="http://www.plantphysiol.org/cgi/doi/10.1104/pp.15.01240">www.plantphysiol.org/cgi/doi/10.1104/pp.15.01240</ext-link></p></fn><corresp id="cor1"><label>*</label>Address correspondence to <email>pfacchin@ucalgary.ca</email>.</corresp><fn id="afn1"><p>The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (<ext-link ext-link-type="uri" xlink:href="http://www.plantphysiol.org">www.plantphysiol.org</ext-link>) is: Peter J. Facchini (<email>pfacchin@ucalgary.ca</email>).</p></fn><fn id="afn2"><p>L.C. conducted most of the experiments and cowrote the article; J.M.H. performed the mass spectrometry analysis; P.J.F. conceived and supervised the research and cowrote the article.</p></fn></author-notes><pmc-comment>Fake ppub date generated by PMC from publisher
pub-date/@pub-type='epub-ppub' </pmc-comment>
<pub-date pub-type="ppub"><month>10</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>21</day><month>8</month><year>2015</year></pub-date><volume>169</volume><issue>2</issue><fpage>1127</fpage><lpage>1140</lpage><history><date date-type="received"><day>06</day><month>8</month><year>2015</year></date><date date-type="accepted"><day>20</day><month>8</month><year>2015</year></date></history><permissions><copyright-statement>© 2015 American Society of Plant Biologists. All Rights Reserved.</copyright-statement><copyright-year>2015</copyright-year></permissions><self-uri xlink:role="icon" xlink:href="PP_PP201501240_ic1.gif"></self-uri><abstract abstract-type="precis"><p>A subset of multifunctional O-methyltransferases is involved in the formation of the tetra-O-methylated benzylisoquinoline alkaloid glaucine.</p></abstract><abstract><p>Transcriptome resources for the medicinal plant <italic>Glaucium flavum</italic> were searched for orthologs showing identity with characterized <italic>O</italic>-methyltransferases (OMTs) involved in benzylisoquinoline alkaloid biosynthesis. Seven recombinant proteins were functionally tested using the signature alkaloid substrates for six OMTs: norlaudanosoline 6-OMT, 6-<italic>O</italic>-methyllaudanosoline 4′-OMT, reticuline 7-OMT, norreticuline 7-OMT, scoulerine 9-OMT, and tetrahydrocolumbamine OMT. A notable alkaloid in yellow horned poppy (<italic>G. flavum</italic> [GFL]) is the aporphine alkaloid glaucine, which displays C8-C6′ coupling and four <italic>O</italic>-methyl groups at C6, C7, C3′, and C4′ as numbered on the 1-benzylisoquinoline scaffold. Three recombinant enzymes accepted 1-benzylisoquinolines with differential substrate and regiospecificity. GFLOMT2 displayed the highest amino acid sequence identity with norlaudanosoline 6-OMT, showed a preference for the 6-<italic>O</italic>-methylation of norlaudanosoline, and <italic>O</italic>-methylated the 3′ and 4′ hydroxyl groups of certain alkaloids. GFLOMT1 showed the highest sequence identity with 6-<italic>O</italic>-methyllaudanosoline 4′OMT and catalyzed the 6-<italic>O</italic>-methylation of norlaudanosoline, but more efficiently 4′-<italic>O</italic>-methylated the GFLOMT2 reaction product 6-<italic>O</italic>-methylnorlaudanosoline and its <italic>N</italic>-methylated derivative 6-<italic>O</italic>-methyllaudanosoline. GFLOMT1 also effectively 3′-<italic>O</italic>-methylated both reticuline and norreticuline. GFLOMT6 was most similar to scoulerine 9-OMT and efficiently catalyzed both 3′- and 7′-<italic>O</italic>-methylations of several 1-benzylisoquinolines, with a preference for <italic>N</italic>-methylated substrates. All active enzymes accepted scoulerine and tetrahydrocolumbamine. Exogenous norlaudanosoline was converted to tetra-<italic>O</italic>-methylated laudanosine using combinations of <italic>Escherichia coli</italic> producing (1) GFLOMT1, (2) either GFLOMT2 or GFLOMT6, and (3) coclaurine <italic>N</italic>-methyltransferase from <italic>Coptis japonica</italic>. Expression profiles of <italic>GFLOMT1</italic>, <italic>GFLOMT2</italic>, and <italic>GFLOMT6</italic> in different plant organs were in agreement with the <italic>O</italic>-methylation patterns of alkaloids in <italic>G. flavum</italic> determined by high-resolution, Fourier-transform mass spectrometry.</p></abstract><counts><page-count count="14"></page-count></counts><custom-meta-group><custom-meta><meta-name> DJS Export </meta-name><meta-value>v1</meta-value></custom-meta></custom-meta-group></article-meta><notes><glossary><title>Glossary</title><def-list><def-item><term id="term1">BIA</term><def id="def1"><p>benzylisoquinoline alkaloid</p></def></def-item><def-item><term id="term2">SAM</term><def id="def2"><p><italic>S</italic>-adenosyl-<sc>l</sc>-Met</p></def></def-item><def-item><term id="term3">cDNA</term><def id="def3"><p>complementary DNA</p></def></def-item><def-item><term id="term4">LC</term><def id="def4"><p>liquid chromatography</p></def></def-item><def-item><term id="term5">MS/MS</term><def id="def5"><p>tandem mass spectrometry</p></def></def-item><def-item><term id="term6">CID</term><def id="def6"><p>collision-induced dissociation</p></def></def-item><def-item><term id="term7"><italic>m</italic>/<italic>z</italic></term><def id="def7"><p>mass-to-charge ratio</p></def></def-item><def-item><term id="term8">FTMS</term><def id="def8"><p>Fourier-transform mass spectrometry</p></def></def-item><def-item><term id="term9">IPTG</term><def id="def9"><p>isopropyl β-<sc>d</sc>-thiogalactopyranoside</p></def></def-item></def-list></glossary></notes></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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