127 lines
12 KiB
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127 lines
12 KiB
XML
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<mods:title id="399419128EFD99B6F2035CB0AE42131E">Biosynthesis of methyl (E) - cinnamate in the liverwort Conocephalum salebrosum and evolution of cinnamic acid methyltransferase</mods:title>
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<mods:namePart id="9F6593267179E25CD07A62F290B90C10">Zhang, Chi</mods:namePart>
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<mods:affiliation id="BE8019F40A5BF38E5A0293CC2834EFF9">∗ & Department of Plant Sciences, University of Tennessee, Knoxville, TN 37996, USA</mods:affiliation>
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<mods:namePart id="DF52BA42F116405CFE9EB466CAA08008">Chen, Xinlu</mods:namePart>
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<mods:namePart id="89ABB5D6A093F7C4B235D88481FFAB66">Crandall-Stotler, Barbara</mods:namePart>
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<mods:namePart id="D8C6E2181AFBE6675C8AB1567BD4532A">Qian, Ping</mods:namePart>
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<mods:namePart id="AF85BF351A0336654877BCADB6544893">Köllner, Tobias G.</mods:namePart>
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<mods:namePart id="5992D308CD298A0D6DAE2C05283F20D7">Guo, Hong</mods:namePart>
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<mods:namePart id="09901CF43CEF579367877486DDB659F7">Chen, Feng</mods:namePart>
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<mods:title id="B44122CED31705BF98CC08018A1D5093">Phytochemistry</mods:title>
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<mods:date id="12A9BD871020552454E34F1D50CE4D35">2019</mods:date>
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<mods:number id="C8B216B887D549A0FC7DB6F80EEF86B9">2019-08-31</mods:number>
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<mods:number id="04F4D682DC1DC1B86A875CDC32555BC3">164</mods:number>
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<mods:url id="D941793454DF75F8DAF86F8DEF7C7B0E">http://dx.doi.org/10.1016/j.phytochem.2019.04.013</mods:url>
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<mods:classification id="AA75812888A5E747E0056DD0EA5254ED">journal article</mods:classification>
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<mods:identifier id="1434881E4F61B654887F25E800075A59" type="DOI">10.1016/j.phytochem.2019.04.013</mods:identifier>
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<mods:identifier id="9BDF4FF33ABAE98AB11AEA121F56B397" type="ISSN">1873-3700</mods:identifier>
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<treatment id="03AB0102996FE01BAB4B0F80FEFF3D18" LSID="urn:lsid:plazi:treatment:03AB0102996FE01BAB4B0F80FEFF3D18" httpUri="http://treatment.plazi.org/id/03AB0102996FE01BAB4B0F80FEFF3D18" lastPageNumber="53" pageId="3" pageNumber="53">
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<subSubSection id="C318E39F996FE01BAB4B0F80FD2C3A9E" box="[100,724,687,706]" pageId="3" pageNumber="53" type="nomenclature">
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<heading id="D0F50778996FE01BAB4B0F80FD2C3A9E" bold="true" box="[100,724,687,706]" fontSize="36" level="1" pageId="3" pageNumber="53" reason="1">
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<emphasis id="B9766C06996FE01BAB4B0F80FD2C3A9E" bold="true" box="[100,724,687,706]" italics="true" pageId="3" pageNumber="53">
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2.3. Biochemical characterization of CsSABATHs expressed in
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<taxonomicName id="4C02CB97996FE01BA9B30F80FD2C3A9E" ID-CoL="3BGTD" ID-ENA="1010795" authorityName="Castellani & Chalmers" authorityYear="1919" baseAuthorityName="Migula" baseAuthorityYear="1895" box="[668,724,687,706]" class="Gammaproteobacteria" family="Enterobacteriaceae" genus="Escherichia" kingdom="Bacteria" order="Enterobacteriales" pageId="3" pageNumber="53" phylum="Proteobacteria" rank="species" species="coli">E. coli</taxonomicName>
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</emphasis>
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</heading>
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</paragraph>
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<subSubSection id="C318E39F996FE01BABAA0FC8FEFF3D18" pageId="3" pageNumber="53" type="description">
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<paragraph id="8BBDB014996FE01BABAA0FC8FEFF3D18" blockId="3.[100,771,743,1348]" pageId="3" pageNumber="53">
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Gene expression analysis (
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<figureCitation id="1339AC91996FE01BAAB80FC8FE2D3AA6" box="[407,469,743,762]" captionStart="Fig" captionStartId="3.[100,130,369,386]" captionTargetBox="[106,761,152,337]" captionTargetId="graphics-1083@3.[272,761,152,279]" captionTargetPageId="3" captionText="Fig. 3. Expression of six CsSABATHs genes in sterile thalli measured by semiquantitative RT-PCR. Same amount of cDNA was used in each reaction. This experiment was repeated three times with similar results. “M” indicates molecular marker." figureDoi="http://doi.org/10.5281/zenodo.10483038" httpUri="https://zenodo.org/record/10483038/files/figure.png" pageId="3" pageNumber="53">Fig. 3</figureCitation>
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) suggested that
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<emphasis id="B9766C06996FE01BA9A50FC8FD043AA6" bold="true" box="[650,764,743,762]" italics="true" pageId="3" pageNumber="53">CsSABATH2</emphasis>
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,
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<emphasis id="B9766C06996FE01BAB4B0E2CFF2E3B4A" bold="true" box="[100,214,771,790]" italics="true" pageId="3" pageNumber="53">CsSABATH4</emphasis>
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and
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<emphasis id="B9766C06996FE01BAA3D0E2CFE7B3B4A" bold="true" box="[274,387,771,790]" italics="true" pageId="3" pageNumber="53">CsSABATH6</emphasis>
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are the most probable candidates as
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<emphasis id="B9766C06996FE01BAB4B0E30FF663B6E" bold="true" box="[100,158,799,818]" italics="true" pageId="3" pageNumber="53">CAMT</emphasis>
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. To validate this prediction, we characterized the proteins encoded by all six
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<emphasis id="B9766C06996FE01BAA2C0E14FE913B12" bold="true" box="[259,361,827,846]" italics="true" pageId="3" pageNumber="53">CsSABATH</emphasis>
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genes using a biochemical approach. Full-length cDNA for each of the six
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<emphasis id="B9766C06996FE01BAAA40E79FE093B35" bold="true" box="[395,497,854,873]" italics="true" pageId="3" pageNumber="53">CsSABATH</emphasis>
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genes was cloned by RT-PCR into a protein expression vector without any tag and expressed in
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<taxonomicName id="4C02CB97996FE01BA9E40E5CFCFA3BD9" authorityName="Castellani & Chalmers" authorityYear="1919" baseAuthorityName="Migula" baseAuthorityYear="1895" box="[715,770,882,902]" class="Gammaproteobacteria" family="Enterobacteriaceae" genus="Escherichia" kingdom="Bacteria" order="Enterobacteriales" pageId="3" pageNumber="53" phylum="Proteobacteria" rank="species" species="coli">
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<emphasis id="B9766C06996FE01BA9E40E5CFCFA3BD9" bold="true" box="[715,770,882,902]" italics="true" pageId="3" pageNumber="53">E. coli</emphasis>
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</taxonomicName>
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to produce recombinant proteins. Each of the recombinant CsSABATH enzymes was assayed with (
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<emphasis id="B9766C06996FE01BAA560E85FE7D3BE1" bold="true" box="[377,389,938,957]" italics="true" pageId="3" pageNumber="53">E</emphasis>
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)-cinnamic acid and an additional nine carboxyl acids: indole-3-acetic acid, gibberellin A3, salicylic acid, jasmonic acid, anthranilic acid, nicotinic acid, benzoic acid,
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<emphasis id="B9766C06996FE01BA9B60ECDFD5B3BA9" bold="true" box="[665,675,994,1013]" italics="true" pageId="3" pageNumber="53">p</emphasis>
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-coumaric acid and abscisic acid (
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<tableCitation id="C68085AF996FE01BAA600ED1FE623C4D" box="[335,410,1022,1041]" captionStart="Table 1" captionStartId="3.[100,150,1537,1553]" captionTargetPageId="3" captionText="Table 1 The relative activities of CsSABATH4 and CsSABATH6 from C. salebrosum with ten carboxyl acids." pageId="3" pageNumber="53">Table 1</tableCitation>
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). Among the six CsSABATHs, CsSABATH6 was highly active using (
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<emphasis id="B9766C06996FE01BAA8E0935FE553C71" bold="true" box="[417,429,1050,1069]" italics="true" pageId="3" pageNumber="53">E</emphasis>
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)-cinnamic acid as substrate. It also showed activity with benzoic acid and
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<emphasis id="B9766C06996FE01BAAC00919FE013C15" bold="true" box="[495,505,1078,1097]" italics="true" pageId="3" pageNumber="53">p</emphasis>
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-coumaric acid, which was about 32% and 18% of the activity with (
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<emphasis id="B9766C06996FE01BAAC9097DFE0A3C39" bold="true" box="[486,498,1106,1125]" italics="true" pageId="3" pageNumber="53">E</emphasis>
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)-cinnamic acid. CsSABATH4 also showed some activity with (
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<emphasis id="B9766C06996FE01BAAB30941FE503CDD" bold="true" box="[412,424,1134,1153]" italics="true" pageId="3" pageNumber="53">E</emphasis>
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)-cinnamic acid, but the activity was very low. Instead, CsSABATH4 was most active with salicylic acid as substrate. Its activity with (
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<emphasis id="B9766C06996FE01BAA480989FE8B3CE5" bold="true" box="[359,371,1190,1209]" italics="true" pageId="3" pageNumber="53">E</emphasis>
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)-cinnamic acid was only about 6% of that with salicylic acid. CsSABATH6 and CsSABATH4 were renamed CsCAMT (GenBank accession no. MK673137) and CsSAMT (GeneBank accession no. MK673138), respectively. CsSABATH1, CsSABATH2, CsSABATH3 and CsSABATH5 did not show activity with any of the substrates tested.
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</paragraph>
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</subSubSection>
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</treatment>
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