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Evolution and Function of the Populus SABATH Family Reveal That a Single Amino Acid Change Results in a Substrate Switch.

Identifieur interne : 000F14 ( Main/Exploration ); précédent : 000F13; suivant : 000F15

Evolution and Function of the Populus SABATH Family Reveal That a Single Amino Acid Change Results in a Substrate Switch.

Auteurs : Xue-Min Han [République populaire de Chine] ; Qi Yang [République populaire de Chine] ; Yan-Jing Liu [République populaire de Chine] ; Zhi-Ling Yang [République populaire de Chine] ; Xiao-Ru Wang [République populaire de Chine] ; Qing-Yin Zeng [République populaire de Chine] ; Hai-Ling Yang [République populaire de Chine]

Source :

RBID : pubmed:29237058

Descripteurs français

English descriptors

Abstract

Evolutionary mechanisms of substrate specificities of enzyme families remain poorly understood. Plant SABATH methyltransferases catalyze methylation of the carboxyl group of various low molecular weight metabolites. Investigation of the functional diversification of the SABATH family in plants could shed light on the evolution of substrate specificities in this enzyme family. Previous studies identified 28 SABATH genes from the Populus trichocarpa genome. In this study, we re-annotated the Populus SABATH gene family, and performed molecular evolution, gene expression and biochemical analyses of this large gene family. Twenty-eight Populus SABATH genes were divided into three classes with distinct divergences in their gene structure, expression responses to abiotic stressors and enzymatic properties of encoded proteins. Populus class I SABATH proteins converted IAA to methyl-IAA, class II SABATH proteins converted benzoic acid (BA) and salicylic acid (SA) to methyl-BA and methyl-SA, while class III SABATH proteins converted farnesoic acid (FA) to methyl-FA. For Populus class II SABATH proteins, both forward and reverse mutagenesis studies showed that a single amino acid switch between PtSABATH4 and PtSABATH24 resulted in substrate switch. Our findings provide new insights into the evolution of substrate specificities of enzyme families.

DOI: 10.1093/pcp/pcx198
PubMed: 29237058


Affiliations:


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Le document en format XML

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<term>Chromosomes, Plant (genetics)</term>
<term>Evolution, Molecular (MeSH)</term>
<term>Gas Chromatography-Mass Spectrometry (MeSH)</term>
<term>Gene Expression Regulation, Plant (MeSH)</term>
<term>Genes, Plant (MeSH)</term>
<term>Methyltransferases (chemistry)</term>
<term>Methyltransferases (genetics)</term>
<term>Methyltransferases (metabolism)</term>
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<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Populus (genetics)</term>
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<term>Acides aminés (génétique)</term>
<term>Chromatographie gazeuse-spectrométrie de masse (MeSH)</term>
<term>Chromosomes de plante (génétique)</term>
<term>Famille multigénique (MeSH)</term>
<term>Gènes de plante (MeSH)</term>
<term>Methyltransferases (composition chimique)</term>
<term>Methyltransferases (génétique)</term>
<term>Methyltransferases (métabolisme)</term>
<term>Mutagenèse dirigée (MeSH)</term>
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<term>Populus (enzymologie)</term>
<term>Populus (génétique)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Régulation de l'expression des gènes végétaux (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
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<term>Populus</term>
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<term>Acides aminés</term>
<term>Chromosomes de plante</term>
<term>Methyltransferases</term>
<term>Populus</term>
<term>Protéines végétales</term>
<term>Stress physiologique</term>
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<term>Plant Proteins</term>
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<term>Spécificité du substrat</term>
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<term>Séquence d'acides aminés</term>
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<div type="abstract" xml:lang="en">Evolutionary mechanisms of substrate specificities of enzyme families remain poorly understood. Plant SABATH methyltransferases catalyze methylation of the carboxyl group of various low molecular weight metabolites. Investigation of the functional diversification of the SABATH family in plants could shed light on the evolution of substrate specificities in this enzyme family. Previous studies identified 28 SABATH genes from the Populus trichocarpa genome. In this study, we re-annotated the Populus SABATH gene family, and performed molecular evolution, gene expression and biochemical analyses of this large gene family. Twenty-eight Populus SABATH genes were divided into three classes with distinct divergences in their gene structure, expression responses to abiotic stressors and enzymatic properties of encoded proteins. Populus class I SABATH proteins converted IAA to methyl-IAA, class II SABATH proteins converted benzoic acid (BA) and salicylic acid (SA) to methyl-BA and methyl-SA, while class III SABATH proteins converted farnesoic acid (FA) to methyl-FA. For Populus class II SABATH proteins, both forward and reverse mutagenesis studies showed that a single amino acid switch between PtSABATH4 and PtSABATH24 resulted in substrate switch. Our findings provide new insights into the evolution of substrate specificities of enzyme families.</div>
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<AbstractText>Evolutionary mechanisms of substrate specificities of enzyme families remain poorly understood. Plant SABATH methyltransferases catalyze methylation of the carboxyl group of various low molecular weight metabolites. Investigation of the functional diversification of the SABATH family in plants could shed light on the evolution of substrate specificities in this enzyme family. Previous studies identified 28 SABATH genes from the Populus trichocarpa genome. In this study, we re-annotated the Populus SABATH gene family, and performed molecular evolution, gene expression and biochemical analyses of this large gene family. Twenty-eight Populus SABATH genes were divided into three classes with distinct divergences in their gene structure, expression responses to abiotic stressors and enzymatic properties of encoded proteins. Populus class I SABATH proteins converted IAA to methyl-IAA, class II SABATH proteins converted benzoic acid (BA) and salicylic acid (SA) to methyl-BA and methyl-SA, while class III SABATH proteins converted farnesoic acid (FA) to methyl-FA. For Populus class II SABATH proteins, both forward and reverse mutagenesis studies showed that a single amino acid switch between PtSABATH4 and PtSABATH24 resulted in substrate switch. Our findings provide new insights into the evolution of substrate specificities of enzyme families.</AbstractText>
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<DescriptorName UI="D012641" MajorTopicYN="N">Selection, Genetic</DescriptorName>
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<DescriptorName UI="D013312" MajorTopicYN="N">Stress, Physiological</DescriptorName>
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<DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName>
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</MedlineCitation>
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<PubMedPubDate PubStatus="received">
<Year>2017</Year>
<Month>07</Month>
<Day>13</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted">
<Year>2017</Year>
<Month>12</Month>
<Day>08</Day>
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<PubMedPubDate PubStatus="medline">
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<Year>2017</Year>
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<ArticleId IdType="pubmed">29237058</ArticleId>
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<ArticleId IdType="doi">10.1093/pcp/pcx198</ArticleId>
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<country>
<li>République populaire de Chine</li>
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<li>Pékin</li>
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<country name="République populaire de Chine">
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<name sortKey="Han, Xue Min" sort="Han, Xue Min" uniqKey="Han X" first="Xue-Min" last="Han">Xue-Min Han</name>
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<name sortKey="Liu, Yan Jing" sort="Liu, Yan Jing" uniqKey="Liu Y" first="Yan-Jing" last="Liu">Yan-Jing Liu</name>
<name sortKey="Wang, Xiao Ru" sort="Wang, Xiao Ru" uniqKey="Wang X" first="Xiao-Ru" last="Wang">Xiao-Ru Wang</name>
<name sortKey="Yang, Hai Ling" sort="Yang, Hai Ling" uniqKey="Yang H" first="Hai-Ling" last="Yang">Hai-Ling Yang</name>
<name sortKey="Yang, Qi" sort="Yang, Qi" uniqKey="Yang Q" first="Qi" last="Yang">Qi Yang</name>
<name sortKey="Yang, Zhi Ling" sort="Yang, Zhi Ling" uniqKey="Yang Z" first="Zhi-Ling" last="Yang">Zhi-Ling Yang</name>
<name sortKey="Zeng, Qing Yin" sort="Zeng, Qing Yin" uniqKey="Zeng Q" first="Qing-Yin" last="Zeng">Qing-Yin Zeng</name>
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