Evolutionary origin of O-acetyltransferases responsible for glucomannan acetylation in land plants.
Identifieur interne : 000972 ( Main/Exploration ); précédent : 000971; suivant : 000973Evolutionary origin of O-acetyltransferases responsible for glucomannan acetylation in land plants.
Auteurs : Ruiqin Zhong [États-Unis] ; Dongtao Cui [États-Unis] ; Zheng-Hua Ye [États-Unis]Source :
- The New phytologist [ 1469-8137 ] ; 2019.
Descripteurs français
- KwdFr :
- Acetyltransferases (génétique), Acetyltransferases (métabolisme), Acétylation (MeSH), Biocatalyse (MeSH), Cellules HEK293 (MeSH), Embryophyta (enzymologie), Embryophyta (génétique), Gènes de plante (MeSH), Humains (MeSH), Mannanes (métabolisme), Phylogenèse (MeSH), Protéines recombinantes (biosynthèse), Spectroscopie par résonance magnétique du proton (MeSH), Évolution moléculaire (MeSH).
- MESH :
- biosynthèse : Protéines recombinantes.
- enzymologie : Embryophyta.
- génétique : Acetyltransferases, Embryophyta.
- métabolisme : Acetyltransferases, Mannanes.
- Acétylation, Biocatalyse, Cellules HEK293, Gènes de plante, Humains, Phylogenèse, Spectroscopie par résonance magnétique du proton, Évolution moléculaire.
English descriptors
- KwdEn :
- Acetylation (MeSH), Acetyltransferases (genetics), Acetyltransferases (metabolism), Biocatalysis (MeSH), Embryophyta (enzymology), Embryophyta (genetics), Evolution, Molecular (MeSH), Genes, Plant (MeSH), HEK293 Cells (MeSH), Humans (MeSH), Mannans (metabolism), Phylogeny (MeSH), Proton Magnetic Resonance Spectroscopy (MeSH), Recombinant Proteins (biosynthesis).
- MESH :
- chemical , biosynthesis : Recombinant Proteins.
- chemical , genetics : Acetyltransferases.
- chemical , metabolism : Acetyltransferases, Mannans.
- enzymology : Embryophyta.
- genetics : Embryophyta.
- Acetylation, Biocatalysis, Evolution, Molecular, Genes, Plant, HEK293 Cells, Humans, Phylogeny, Proton Magnetic Resonance Spectroscopy.
Abstract
Mannans are an abundant cell wall polysaccharide in bryophytes, seedless vascular plants and gymnosperms. A previous study has shown that mannan acetylation in Arabidopsis and konjac is mediated by mannan O-acetyltransferases belonging to the Domain of Unknown Function (DUF) 231 family. However, little is known about the acetylation patterns of mannans in bryophytes and seedless vascular plants, and the evolutionary origin of mannan O-acetyltransferases in land plants has not yet been studied. Phylogenetic analysis of the DUF231 family revealed that DUF231 members were present in the charophycean green algae and evolved to form overlapped and divergent phylogenetic groups in different taxa of land plants. Acetyltransferase activity assays of recombinant proteins demonstrated that a number of group II DUF231 members from moss, Selaginella, pine, spruce, rice and poplar were mannan 2-O- and 3-O-acetyltransferases, whereas the two group I DUF231 members from the alga Klebsormidium nitens were not. Structural analysis of mannans from moss and Selaginella showed they were composed of mannosyl and glucosyl residues and the mannosyl residues were acetylated at O-2 and O-3. These findings indicate that although the DUF231 genes originated in algae, their recruitment as mannan O-acetyltransferases probably occurred in bryophytes, and the biochemical functions of these O-acetyltransferases are evolutionarily conserved throughout land plants.
DOI: 10.1111/nph.15988
PubMed: 31183872
Affiliations:
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(biosynthèse)</term><term>Spectroscopie par résonance magnétique du proton (MeSH)</term><term>Évolution moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Acetyltransferases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acetyltransferases</term><term>Mannans</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Embryophyta</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Embryophyta</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Embryophyta</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Acetyltransferases</term><term>Embryophyta</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acetyltransferases</term><term>Mannanes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Acetylation</term><term>Biocatalysis</term><term>Evolution, Molecular</term><term>Genes, Plant</term><term>HEK293 Cells</term><term>Humans</term><term>Phylogeny</term><term>Proton Magnetic Resonance Spectroscopy</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acétylation</term><term>Biocatalyse</term><term>Cellules HEK293</term><term>Gènes de plante</term><term>Humains</term><term>Phylogenèse</term><term>Spectroscopie par résonance magnétique du proton</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mannans are an abundant cell wall polysaccharide in bryophytes, seedless vascular plants and gymnosperms. A previous study has shown that mannan acetylation in Arabidopsis and konjac is mediated by mannan O-acetyltransferases belonging to the Domain of Unknown Function (DUF) 231 family. However, little is known about the acetylation patterns of mannans in bryophytes and seedless vascular plants, and the evolutionary origin of mannan O-acetyltransferases in land plants has not yet been studied. Phylogenetic analysis of the DUF231 family revealed that DUF231 members were present in the charophycean green algae and evolved to form overlapped and divergent phylogenetic groups in different taxa of land plants. Acetyltransferase activity assays of recombinant proteins demonstrated that a number of group II DUF231 members from moss, Selaginella, pine, spruce, rice and poplar were mannan 2-O- and 3-O-acetyltransferases, whereas the two group I DUF231 members from the alga Klebsormidium nitens were not. Structural analysis of mannans from moss and Selaginella showed they were composed of mannosyl and glucosyl residues and the mannosyl residues were acetylated at O-2 and O-3. These findings indicate that although the DUF231 genes originated in algae, their recruitment as mannan O-acetyltransferases probably occurred in bryophytes, and the biochemical functions of these O-acetyltransferases are evolutionarily conserved throughout land plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31183872</PMID><DateCompleted><Year>2020</Year><Month>05</Month><Day>04</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-8137</ISSN><JournalIssue CitedMedium="Internet"><Volume>224</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>10</Month></PubDate></JournalIssue><Title>The New phytologist</Title><ISOAbbreviation>New Phytol</ISOAbbreviation></Journal><ArticleTitle>Evolutionary origin of O-acetyltransferases responsible for glucomannan acetylation in land plants.</ArticleTitle><Pagination><MedlinePgn>466-479</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/nph.15988</ELocationID><Abstract><AbstractText>Mannans are an abundant cell wall polysaccharide in bryophytes, seedless vascular plants and gymnosperms. A previous study has shown that mannan acetylation in Arabidopsis and konjac is mediated by mannan O-acetyltransferases belonging to the Domain of Unknown Function (DUF) 231 family. However, little is known about the acetylation patterns of mannans in bryophytes and seedless vascular plants, and the evolutionary origin of mannan O-acetyltransferases in land plants has not yet been studied. Phylogenetic analysis of the DUF231 family revealed that DUF231 members were present in the charophycean green algae and evolved to form overlapped and divergent phylogenetic groups in different taxa of land plants. Acetyltransferase activity assays of recombinant proteins demonstrated that a number of group II DUF231 members from moss, Selaginella, pine, spruce, rice and poplar were mannan 2-O- and 3-O-acetyltransferases, whereas the two group I DUF231 members from the alga Klebsormidium nitens were not. Structural analysis of mannans from moss and Selaginella showed they were composed of mannosyl and glucosyl residues and the mannosyl residues were acetylated at O-2 and O-3. These findings indicate that although the DUF231 genes originated in algae, their recruitment as mannan O-acetyltransferases probably occurred in bryophytes, and the biochemical functions of these O-acetyltransferases are evolutionarily conserved throughout land plants.</AbstractText><CopyrightInformation>© 2019 The Authors. New Phytologist © 2019 New Phytologist Trust.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhong</LastName><ForeName>Ruiqin</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Plant Biology, University of Georgia, Athens, GA, 30602, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cui</LastName><ForeName>Dongtao</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Georgia, Athens, GA, 30602, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ye</LastName><ForeName>Zheng-Hua</ForeName><Initials>ZH</Initials><Identifier Source="ORCID">0000-0001-5714-744X</Identifier><AffiliationInfo><Affiliation>Department of Plant Biology, University of Georgia, Athens, GA, 30602, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>MK876266</AccessionNumber><AccessionNumber>MK876267</AccessionNumber><AccessionNumber>MK876268</AccessionNumber><AccessionNumber>MK876269</AccessionNumber><AccessionNumber>MK876270</AccessionNumber><AccessionNumber>MK876271</AccessionNumber><AccessionNumber>MK876272</AccessionNumber><AccessionNumber>MK876273</AccessionNumber><AccessionNumber>MK876274</AccessionNumber><AccessionNumber>MK876275</AccessionNumber><AccessionNumber>MK876276</AccessionNumber><AccessionNumber>MK876277</AccessionNumber><AccessionNumber>MK876278</AccessionNumber><AccessionNumber>MK876279</AccessionNumber><AccessionNumber>MK876280</AccessionNumber><AccessionNumber>MK876281</AccessionNumber><AccessionNumber>MK876282</AccessionNumber><AccessionNumber>MK876283</AccessionNumber><AccessionNumber>MK876284</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>07</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>New Phytol</MedlineTA><NlmUniqueID>9882884</NlmUniqueID><ISSNLinking>0028-646X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008351">Mannans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>36W3E5TAMG</RegistryNumber><NameOfSubstance UI="C022901">(1-6)-alpha-glucomannan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.1.-</RegistryNumber><NameOfSubstance UI="D000123">Acetyltransferases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000107" MajorTopicYN="N">Acetylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000123" MajorTopicYN="N">Acetyltransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019669" MajorTopicYN="N">Embryophyta</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="Y">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017343" MajorTopicYN="N">Genes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008351" MajorTopicYN="N">Mannans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D066244" MajorTopicYN="N">Proton Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Selaginella
</Keyword><Keyword MajorTopicYN="Y">DUF231</Keyword><Keyword MajorTopicYN="Y">acetyltransferase</Keyword><Keyword MajorTopicYN="Y">cell wall</Keyword><Keyword MajorTopicYN="Y">mannan</Keyword><Keyword MajorTopicYN="Y">moss</Keyword><Keyword MajorTopicYN="Y">pine</Keyword><Keyword MajorTopicYN="Y">spruce</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>03</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>06</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>6</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>5</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>6</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31183872</ArticleId><ArticleId IdType="doi">10.1111/nph.15988</ArticleId></ArticleIdList><ReferenceList><Title>References</Title><Reference><Citation>Bischoff V, Nita S, Neumetzler L, Schindelasch D, Urbain A, Eshed R, Persson S, Delmer D, Scheible WR. 2010. 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Plant Cell Physiology 58: 156-174.</Citation></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Zhong, Ruiqin" sort="Zhong, Ruiqin" uniqKey="Zhong R" first="Ruiqin" last="Zhong">Ruiqin Zhong</name></noRegion><name sortKey="Cui, Dongtao" sort="Cui, Dongtao" uniqKey="Cui D" first="Dongtao" last="Cui">Dongtao Cui</name><name sortKey="Ye, Zheng Hua" sort="Ye, Zheng Hua" uniqKey="Ye Z" first="Zheng-Hua" last="Ye">Zheng-Hua Ye</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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