Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis.
Identifieur interne : 002339 ( Main/Exploration ); précédent : 002338; suivant : 002340Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis.
Auteurs : Beatriz Sánchez-Parra [Espagne] ; Henning Frerigmann [Allemagne] ; Marta-Marina Pérez Alonso [Espagne] ; Víctor Carrasco Loba [Espagne] ; Ricarda Jost [Australie] ; Mathias Hentrich [Allemagne] ; Stephan Pollmann [Espagne]Source :
- Plants (Basel, Switzerland) [ 2223-7747 ] ; 2014.
Abstract
Amidases [EC 3.5.1.4] capable of converting indole-3-acetamide (IAM) into the major plant growth hormone indole-3-acetic acid (IAA) are assumed to be involved in auxin de novo biosynthesis. With the emerging amount of genomics data, it was possible to identify over forty proteins with substantial homology to the already characterized amidases from Arabidopsis and tobacco. The observed high conservation of amidase-like proteins throughout the plant kingdom may suggest an important role of theses enzymes in plant development. Here, we report cloning and functional analysis of four, thus far, uncharacterized plant amidases from Oryza sativa, Sorghum bicolor, Medicago truncatula, and Populus trichocarpa. Intriguingly, we were able to demonstrate that the examined amidases are also capable of converting phenyl-2-acetamide (PAM) into phenyl-2-acetic acid (PAA), an auxin endogenous to several plant species including Arabidopsis. Furthermore, we compared the subcellular localization of the enzymes to that of Arabidopsis AMI1, providing further evidence for similar enzymatic functions. Our results point to the presence of a presumably conserved pathway of auxin biosynthesis via IAM, as amidases, both of monocot, and dicot origins, were analyzed.
DOI: 10.3390/plants3030324
PubMed: 27135507
PubMed Central: PMC4844348
Affiliations:
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M-40, km 38, 28223 Pozuelo de Alarcón (Madrid), Spain. beatriz.sanchez@upm.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid)</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Frerigmann, Henning" sort="Frerigmann, Henning" uniqKey="Frerigmann H" first="Henning" last="Frerigmann">Henning Frerigmann</name><affiliation wicri:level="1"><nlm:affiliation>Department of Plant Physiology, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Universitätsstraße 150, 44801 Bochum, Germany. henning.frerigmann@uni-koeln.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Plant Physiology, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Universitätsstraße 150, 44801 Bochum</wicri:regionArea><wicri:noRegion>44801 Bochum</wicri:noRegion><wicri:noRegion>44801 Bochum</wicri:noRegion><wicri:noRegion>44801 Bochum</wicri:noRegion></affiliation></author><author><name sortKey="Alonso, Marta Marina Perez" sort="Alonso, Marta Marina Perez" uniqKey="Alonso M" first="Marta-Marina Pérez" last="Alonso">Marta-Marina Pérez Alonso</name><affiliation wicri:level="2"><nlm:affiliation>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid), Spain. martamarina.perez@upm.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid)</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Loba, Victor Carrasco" sort="Loba, Victor Carrasco" uniqKey="Loba V" first="Víctor Carrasco" last="Loba">Víctor Carrasco Loba</name><affiliation wicri:level="2"><nlm:affiliation>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid), Spain. victorcarrascoloba@gmail.com.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid)</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Jost, Ricarda" sort="Jost, Ricarda" uniqKey="Jost R" first="Ricarda" last="Jost">Ricarda Jost</name><affiliation wicri:level="1"><nlm:affiliation>School of Plant Biology, University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia. ricarda.jost@uwa.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Plant Biology, University of Western Australia, 35 Stirling Highway, Crawley, WA 6009</wicri:regionArea><wicri:noRegion>WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Hentrich, Mathias" sort="Hentrich, Mathias" uniqKey="Hentrich M" first="Mathias" last="Hentrich">Mathias Hentrich</name><affiliation wicri:level="1"><nlm:affiliation>Department of Plant Physiology, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Universitätsstraße 150, 44801 Bochum, Germany. mathias.hentrich@rub.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Plant Physiology, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Universitätsstraße 150, 44801 Bochum</wicri:regionArea><wicri:noRegion>44801 Bochum</wicri:noRegion><wicri:noRegion>44801 Bochum</wicri:noRegion><wicri:noRegion>44801 Bochum</wicri:noRegion></affiliation></author><author><name sortKey="Pollmann, Stephan" sort="Pollmann, Stephan" uniqKey="Pollmann S" first="Stephan" last="Pollmann">Stephan Pollmann</name><affiliation wicri:level="2"><nlm:affiliation>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid), Spain. stephan.pollmann@upm.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid)</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author></analytic><series><title level="j">Plants (Basel, Switzerland)</title><idno type="ISSN">2223-7747</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Amidases [EC 3.5.1.4] capable of converting indole-3-acetamide (IAM) into the major plant growth hormone indole-3-acetic acid (IAA) are assumed to be involved in auxin de novo biosynthesis. With the emerging amount of genomics data, it was possible to identify over forty proteins with substantial homology to the already characterized amidases from Arabidopsis and tobacco. The observed high conservation of amidase-like proteins throughout the plant kingdom may suggest an important role of theses enzymes in plant development. Here, we report cloning and functional analysis of four, thus far, uncharacterized plant amidases from Oryza sativa, Sorghum bicolor, Medicago truncatula, and Populus trichocarpa. Intriguingly, we were able to demonstrate that the examined amidases are also capable of converting phenyl-2-acetamide (PAM) into phenyl-2-acetic acid (PAA), an auxin endogenous to several plant species including Arabidopsis. Furthermore, we compared the subcellular localization of the enzymes to that of Arabidopsis AMI1, providing further evidence for similar enzymatic functions. Our results point to the presence of a presumably conserved pathway of auxin biosynthesis via IAM, as amidases, both of monocot, and dicot origins, were analyzed. </div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">27135507</PMID><DateCompleted><Year>2016</Year><Month>05</Month><Day>04</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2223-7747</ISSN><JournalIssue CitedMedium="Print"><Volume>3</Volume><Issue>3</Issue><PubDate><Year>2014</Year><Month>Aug</Month><Day>07</Day></PubDate></JournalIssue><Title>Plants (Basel, Switzerland)</Title><ISOAbbreviation>Plants (Basel)</ISOAbbreviation></Journal><ArticleTitle>Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis.</ArticleTitle><Pagination><MedlinePgn>324-47</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3390/plants3030324</ELocationID><Abstract><AbstractText>Amidases [EC 3.5.1.4] capable of converting indole-3-acetamide (IAM) into the major plant growth hormone indole-3-acetic acid (IAA) are assumed to be involved in auxin de novo biosynthesis. With the emerging amount of genomics data, it was possible to identify over forty proteins with substantial homology to the already characterized amidases from Arabidopsis and tobacco. The observed high conservation of amidase-like proteins throughout the plant kingdom may suggest an important role of theses enzymes in plant development. Here, we report cloning and functional analysis of four, thus far, uncharacterized plant amidases from Oryza sativa, Sorghum bicolor, Medicago truncatula, and Populus trichocarpa. Intriguingly, we were able to demonstrate that the examined amidases are also capable of converting phenyl-2-acetamide (PAM) into phenyl-2-acetic acid (PAA), an auxin endogenous to several plant species including Arabidopsis. Furthermore, we compared the subcellular localization of the enzymes to that of Arabidopsis AMI1, providing further evidence for similar enzymatic functions. Our results point to the presence of a presumably conserved pathway of auxin biosynthesis via IAM, as amidases, both of monocot, and dicot origins, were analyzed. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sánchez-Parra</LastName><ForeName>Beatriz</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid), Spain. beatriz.sanchez@upm.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Frerigmann</LastName><ForeName>Henning</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Plant Physiology, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Universitätsstraße 150, 44801 Bochum, Germany. henning.frerigmann@uni-koeln.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Alonso</LastName><ForeName>Marta-Marina Pérez</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid), Spain. martamarina.perez@upm.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Loba</LastName><ForeName>Víctor Carrasco</ForeName><Initials>VC</Initials><AffiliationInfo><Affiliation>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid), Spain. victorcarrascoloba@gmail.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jost</LastName><ForeName>Ricarda</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>School of Plant Biology, University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia. ricarda.jost@uwa.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hentrich</LastName><ForeName>Mathias</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Plant Physiology, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Universitätsstraße 150, 44801 Bochum, Germany. mathias.hentrich@rub.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pollmann</LastName><ForeName>Stephan</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Center for Plant Biotechnology and Genomics (U.P.M.-I.N.I.A.), Technical University Madrid, Montegancedo Campus, Crta. M-40, km 38, 28223 Pozuelo de Alarcón (Madrid), Spain. stephan.pollmann@upm.es.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>08</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Plants (Basel)</MedlineTA><NlmUniqueID>101596181</NlmUniqueID><ISSNLinking>2223-7747</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">amidase</Keyword><Keyword MajorTopicYN="N">auxin</Keyword><Keyword MajorTopicYN="N">indole-3-acetamide</Keyword><Keyword MajorTopicYN="N">indole-3-acetic acid</Keyword><Keyword MajorTopicYN="N">phenyl-2-acetamide</Keyword><Keyword MajorTopicYN="N">phenyl-2-acetic acid</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate 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sort="Alonso, Marta Marina Perez" uniqKey="Alonso M" first="Marta-Marina Pérez" last="Alonso">Marta-Marina Pérez Alonso</name><name sortKey="Loba, Victor Carrasco" sort="Loba, Victor Carrasco" uniqKey="Loba V" first="Víctor Carrasco" last="Loba">Víctor Carrasco Loba</name><name sortKey="Pollmann, Stephan" sort="Pollmann, Stephan" uniqKey="Pollmann S" first="Stephan" last="Pollmann">Stephan Pollmann</name></country><country name="Allemagne"><noRegion><name sortKey="Frerigmann, Henning" sort="Frerigmann, Henning" uniqKey="Frerigmann H" first="Henning" last="Frerigmann">Henning Frerigmann</name></noRegion><name sortKey="Hentrich, Mathias" sort="Hentrich, Mathias" uniqKey="Hentrich M" first="Mathias" last="Hentrich">Mathias Hentrich</name></country><country name="Australie"><noRegion><name sortKey="Jost, Ricarda" sort="Jost, Ricarda" uniqKey="Jost R" first="Ricarda" last="Jost">Ricarda Jost</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix 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