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Differential phylogenetic expansions in BAHD acyltransferases across five angiosperm taxa and evidence of divergent expression among Populus paralogues

Identifieur interne : 000493 ( Pmc/Curation ); précédent : 000492; suivant : 000494

Differential phylogenetic expansions in BAHD acyltransferases across five angiosperm taxa and evidence of divergent expression among Populus paralogues

Auteurs : Lindsey K. Tuominen [États-Unis] ; Virgil E. Johnson [États-Unis] ; Chung-Jui Tsai [États-Unis]

Source :

RBID : PMC:3123328

Abstract

Background

BAHD acyltransferases are involved in the synthesis and elaboration of a wide variety of secondary metabolites. Previous research has shown that characterized proteins from this family fall broadly into five major clades and contain two conserved protein motifs. Here, we aimed to expand the understanding of BAHD acyltransferase diversity in plants through genome-wide analysis across five angiosperm taxa. We focus particularly on Populus, a woody perennial known to produce an abundance of secondary metabolites.

Results

Phylogenetic analysis of putative BAHD acyltransferase sequences from Arabidopsis, Medicago, Oryza, Populus, and Vitis, along with previously characterized proteins, supported a refined grouping of eight major clades for this family. Taxon-specific clustering of many BAHD family members appears pervasive in angiosperms. We identified two new multi-clade motifs and numerous clade-specific motifs, several of which have been implicated in BAHD function by previous structural and mutagenesis research. Gene duplication and expression data for Populus-dominated subclades revealed that several paralogous BAHD members in this genus might have already undergone functional divergence.

Conclusions

Differential, taxon-specific BAHD family expansion via gene duplication could be an evolutionary process contributing to metabolic diversity across plant taxa. Gene expression divergence among some Populus paralogues highlights possible distinctions between their biochemical and physiological functions. The newly discovered motifs, especially the clade-specific motifs, should facilitate future functional study of substrate and donor specificity among BAHD enzymes.


Url:
DOI: 10.1186/1471-2164-12-236
PubMed: 21569431
PubMed Central: 3123328

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PMC:3123328

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<p>BAHD acyltransferases are involved in the synthesis and elaboration of a wide variety of secondary metabolites. Previous research has shown that characterized proteins from this family fall broadly into five major clades and contain two conserved protein motifs. Here, we aimed to expand the understanding of BAHD acyltransferase diversity in plants through genome-wide analysis across five angiosperm taxa. We focus particularly on
<italic>Populus</italic>
, a woody perennial known to produce an abundance of secondary metabolites.</p>
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<p>Phylogenetic analysis of putative BAHD acyltransferase sequences from
<italic>Arabidopsis</italic>
,
<italic>Medicago</italic>
,
<italic>Oryza</italic>
,
<italic>Populus</italic>
, and
<italic>Vitis</italic>
, along with previously characterized proteins, supported a refined grouping of eight major clades for this family. Taxon-specific clustering of many BAHD family members appears pervasive in angiosperms. We identified two new multi-clade motifs and numerous clade-specific motifs, several of which have been implicated in BAHD function by previous structural and mutagenesis research. Gene duplication and expression data for
<italic>Populus</italic>
-dominated subclades revealed that several paralogous BAHD members in this genus might have already undergone functional divergence.</p>
</sec>
<sec>
<title>Conclusions</title>
<p>Differential, taxon-specific BAHD family expansion via gene duplication could be an evolutionary process contributing to metabolic diversity across plant taxa. Gene expression divergence among some
<italic>Populus </italic>
paralogues highlights possible distinctions between their biochemical and physiological functions. The newly discovered motifs, especially the clade-specific motifs, should facilitate future functional study of substrate and donor specificity among BAHD enzymes.</p>
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<name sortKey="Ly, E" uniqKey="Ly E">E Ly</name>
</author>
<author>
<name sortKey="Provart, Nj" uniqKey="Provart N">NJ Provart</name>
</author>
</analytic>
</biblStruct>
<biblStruct>
<analytic>
<author>
<name sortKey="Tsai, C J" uniqKey="Tsai C">C-J Tsai</name>
</author>
<author>
<name sortKey="Cseke, Lj" uniqKey="Cseke L">LJ Cseke</name>
</author>
<author>
<name sortKey="Harding, Sa" uniqKey="Harding S">SA Harding</name>
</author>
</analytic>
</biblStruct>
<biblStruct>
<analytic>
<author>
<name sortKey="Ramakers, C" uniqKey="Ramakers C">C Ramakers</name>
</author>
<author>
<name sortKey="Ruijter, Jm" uniqKey="Ruijter J">JM Ruijter</name>
</author>
<author>
<name sortKey="Lekanne Deprez, Rh" uniqKey="Lekanne Deprez R">RH Lekanne Deprez</name>
</author>
<author>
<name sortKey="Moorman, Afm" uniqKey="Moorman A">AFM Moorman</name>
</author>
</analytic>
</biblStruct>
</listBibl>
</div1>
</back>
</TEI>
<pmc article-type="research-article">
<pmc-dir>properties open_access</pmc-dir>
<front>
<journal-meta>
<journal-id journal-id-type="nlm-ta">BMC Genomics</journal-id>
<journal-title-group>
<journal-title>BMC Genomics</journal-title>
</journal-title-group>
<issn pub-type="epub">1471-2164</issn>
<publisher>
<publisher-name>BioMed Central</publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="pmid">21569431</article-id>
<article-id pub-id-type="pmc">3123328</article-id>
<article-id pub-id-type="publisher-id">1471-2164-12-236</article-id>
<article-id pub-id-type="doi">10.1186/1471-2164-12-236</article-id>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Research Article</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>Differential phylogenetic expansions in BAHD acyltransferases across five angiosperm taxa and evidence of divergent expression among
<italic>Populus </italic>
paralogues</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author" id="A1">
<name>
<surname>Tuominen</surname>
<given-names>Lindsey K</given-names>
</name>
<xref ref-type="aff" rid="I1">1</xref>
<email>tuominenl@warnell.uga.edu</email>
</contrib>
<contrib contrib-type="author" id="A2">
<name>
<surname>Johnson</surname>
<given-names>Virgil E</given-names>
</name>
<xref ref-type="aff" rid="I1">1</xref>
<xref ref-type="aff" rid="I2">2</xref>
<email>vedjohns@uga.edu</email>
</contrib>
<contrib contrib-type="author" corresp="yes" id="A3">
<name>
<surname>Tsai</surname>
<given-names>Chung-Jui</given-names>
</name>
<xref ref-type="aff" rid="I1">1</xref>
<xref ref-type="aff" rid="I2">2</xref>
<email>cjtsai@uga.edu</email>
</contrib>
</contrib-group>
<aff id="I1">
<label>1</label>
Warnell School of Forestry and Natural Resources, University of Georgia, Athens, GA 30602-2152, USA</aff>
<aff id="I2">
<label>2</label>
Department of Genetics, University of Georgia, Athens, GA 30602-7223, USA</aff>
<pub-date pub-type="collection">
<year>2011</year>
</pub-date>
<pub-date pub-type="epub">
<day>12</day>
<month>5</month>
<year>2011</year>
</pub-date>
<volume>12</volume>
<fpage>236</fpage>
<lpage>236</lpage>
<history>
<date date-type="received">
<day>9</day>
<month>11</month>
<year>2010</year>
</date>
<date date-type="accepted">
<day>12</day>
<month>5</month>
<year>2011</year>
</date>
</history>
<permissions>
<copyright-statement>Copyright ©2011 Tuominen et al; licensee BioMed Central Ltd.</copyright-statement>
<copyright-year>2011</copyright-year>
<copyright-holder>Tuominen et al; licensee BioMed Central Ltd.</copyright-holder>
<license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/2.0">
<license-p>This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/2.0">http://creativecommons.org/licenses/by/2.0</ext-link>
), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p>
</license>
</permissions>
<self-uri xlink:href="http://www.biomedcentral.com/1471-2164/12/236"></self-uri>
<abstract>
<sec>
<title>Background</title>
<p>BAHD acyltransferases are involved in the synthesis and elaboration of a wide variety of secondary metabolites. Previous research has shown that characterized proteins from this family fall broadly into five major clades and contain two conserved protein motifs. Here, we aimed to expand the understanding of BAHD acyltransferase diversity in plants through genome-wide analysis across five angiosperm taxa. We focus particularly on
<italic>Populus</italic>
, a woody perennial known to produce an abundance of secondary metabolites.</p>
</sec>
<sec>
<title>Results</title>
<p>Phylogenetic analysis of putative BAHD acyltransferase sequences from
<italic>Arabidopsis</italic>
,
<italic>Medicago</italic>
,
<italic>Oryza</italic>
,
<italic>Populus</italic>
, and
<italic>Vitis</italic>
, along with previously characterized proteins, supported a refined grouping of eight major clades for this family. Taxon-specific clustering of many BAHD family members appears pervasive in angiosperms. We identified two new multi-clade motifs and numerous clade-specific motifs, several of which have been implicated in BAHD function by previous structural and mutagenesis research. Gene duplication and expression data for
<italic>Populus</italic>
-dominated subclades revealed that several paralogous BAHD members in this genus might have already undergone functional divergence.</p>
</sec>
<sec>
<title>Conclusions</title>
<p>Differential, taxon-specific BAHD family expansion via gene duplication could be an evolutionary process contributing to metabolic diversity across plant taxa. Gene expression divergence among some
<italic>Populus </italic>
paralogues highlights possible distinctions between their biochemical and physiological functions. The newly discovered motifs, especially the clade-specific motifs, should facilitate future functional study of substrate and donor specificity among BAHD enzymes.</p>
</sec>
</abstract>
</article-meta>
</front>
</pmc>
</record>

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