The cytidine deaminase signature HxE(x)n CxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1.
Identifieur interne : 003466 ( PubMed/Corpus ); précédent : 003465; suivant : 003467The cytidine deaminase signature HxE(x)n CxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1.
Auteurs : Clément Boussardon ; Alexandra Avon ; Peter Kindgren ; Charles S. Bond ; Michael Challenor ; Claire Lurin ; Ian SmallSource :
- The New phytologist [ 1469-8137 ] ; 2014.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Arabidopsis (genetics), Arabidopsis Proteins (chemistry), Arabidopsis Proteins (metabolism), Carrier Proteins (chemistry), Carrier Proteins (metabolism), Cytidine Deaminase (chemistry), Cytidine Deaminase (metabolism), Molecular Sequence Data, Mutation (genetics), Protein Binding, Protein Structure, Tertiary, RNA Editing (genetics), Sequence Alignment, Spectrophotometry, Atomic, Structural Homology, Protein, Structure-Activity Relationship, Tryptophan (metabolism), Zinc (metabolism).
- MESH :
- chemical , chemistry : Arabidopsis Proteins, Carrier Proteins, Cytidine Deaminase.
- genetics : Arabidopsis, Mutation, RNA Editing.
- chemical , metabolism : Arabidopsis Proteins, Carrier Proteins, Cytidine Deaminase, Tryptophan, Zinc.
- Amino Acid Motifs, Amino Acid Sequence, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Spectrophotometry, Atomic, Structural Homology, Protein, Structure-Activity Relationship.
Abstract
In flowering plants, RNA editing involves deamination of specific cytidines to uridines in both mitochondrial and chloroplast transcripts. Pentatricopeptide repeat (PPR) proteins and multiple organellar RNA editing factor (MORF) proteins have been shown to be involved in RNA editing but none have been shown to possess cytidine deaminase activity. The DYW domain of some PPR proteins contains a highly conserved signature resembling the zinc-binding active site motif of known nucleotide deaminases. We modified these highly conserved amino acids in the DYW motif of DYW1, an editing factor required for editing of the ndhD-1 site in Arabidopsis chloroplasts. We demonstrate that several amino acids of this signature motif are required for RNA editing in vivo and for zinc binding in vitro. We conclude that the DYW domain of DYW1 has features in common with cytidine deaminases, reinforcing the hypothesis that this domain forms part of the active enzyme that carries out RNA editing in plants.
DOI: 10.1111/nph.12928
PubMed: 25041347
Links to Exploration step
pubmed:25041347Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The cytidine deaminase signature HxE(x)n CxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1.</title><author><name sortKey="Boussardon, Clement" sort="Boussardon, Clement" uniqKey="Boussardon C" first="Clément" last="Boussardon">Clément Boussardon</name><affiliation><nlm:affiliation>Unité de Recherche en Génomique Végétale (URGV), UMR INRA/UEVE - ERL CNRS, SPS Labex, CP 5708, 91057, Evry Cedex, France; Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, WA, 6009, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Avon, Alexandra" sort="Avon, Alexandra" uniqKey="Avon A" first="Alexandra" last="Avon">Alexandra Avon</name></author><author><name sortKey="Kindgren, Peter" sort="Kindgren, Peter" uniqKey="Kindgren P" first="Peter" last="Kindgren">Peter Kindgren</name></author><author><name sortKey="Bond, Charles S" sort="Bond, Charles S" uniqKey="Bond C" first="Charles S" last="Bond">Charles S. Bond</name></author><author><name sortKey="Challenor, Michael" sort="Challenor, Michael" uniqKey="Challenor M" first="Michael" last="Challenor">Michael Challenor</name></author><author><name sortKey="Lurin, Claire" sort="Lurin, Claire" uniqKey="Lurin C" first="Claire" last="Lurin">Claire Lurin</name></author><author><name sortKey="Small, Ian" sort="Small, Ian" uniqKey="Small I" first="Ian" last="Small">Ian Small</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25041347</idno><idno type="pmid">25041347</idno><idno type="doi">10.1111/nph.12928</idno><idno type="wicri:Area/PubMed/Corpus">003466</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003466</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The cytidine deaminase signature HxE(x)n CxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1.</title><author><name sortKey="Boussardon, Clement" sort="Boussardon, Clement" uniqKey="Boussardon C" first="Clément" last="Boussardon">Clément Boussardon</name><affiliation><nlm:affiliation>Unité de Recherche en Génomique Végétale (URGV), UMR INRA/UEVE - ERL CNRS, SPS Labex, CP 5708, 91057, Evry Cedex, France; Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, WA, 6009, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Avon, Alexandra" sort="Avon, Alexandra" uniqKey="Avon A" first="Alexandra" last="Avon">Alexandra Avon</name></author><author><name sortKey="Kindgren, Peter" sort="Kindgren, Peter" uniqKey="Kindgren P" first="Peter" last="Kindgren">Peter Kindgren</name></author><author><name sortKey="Bond, Charles S" sort="Bond, Charles S" uniqKey="Bond C" first="Charles S" last="Bond">Charles S. Bond</name></author><author><name sortKey="Challenor, Michael" sort="Challenor, Michael" uniqKey="Challenor M" first="Michael" last="Challenor">Michael Challenor</name></author><author><name sortKey="Lurin, Claire" sort="Lurin, Claire" uniqKey="Lurin C" first="Claire" last="Lurin">Claire Lurin</name></author><author><name sortKey="Small, Ian" sort="Small, Ian" uniqKey="Small I" first="Ian" last="Small">Ian Small</name></author></analytic><series><title level="j">The New phytologist</title><idno type="eISSN">1469-8137</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Arabidopsis (genetics)</term><term>Arabidopsis Proteins (chemistry)</term><term>Arabidopsis Proteins (metabolism)</term><term>Carrier Proteins (chemistry)</term><term>Carrier Proteins (metabolism)</term><term>Cytidine Deaminase (chemistry)</term><term>Cytidine Deaminase (metabolism)</term><term>Molecular Sequence Data</term><term>Mutation (genetics)</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>RNA Editing (genetics)</term><term>Sequence Alignment</term><term>Spectrophotometry, Atomic</term><term>Structural Homology, Protein</term><term>Structure-Activity Relationship</term><term>Tryptophan (metabolism)</term><term>Zinc (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arabidopsis Proteins</term><term>Carrier Proteins</term><term>Cytidine Deaminase</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term><term>Mutation</term><term>RNA Editing</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term><term>Carrier Proteins</term><term>Cytidine Deaminase</term><term>Tryptophan</term><term>Zinc</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Spectrophotometry, Atomic</term><term>Structural Homology, Protein</term><term>Structure-Activity Relationship</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In flowering plants, RNA editing involves deamination of specific cytidines to uridines in both mitochondrial and chloroplast transcripts. Pentatricopeptide repeat (PPR) proteins and multiple organellar RNA editing factor (MORF) proteins have been shown to be involved in RNA editing but none have been shown to possess cytidine deaminase activity. The DYW domain of some PPR proteins contains a highly conserved signature resembling the zinc-binding active site motif of known nucleotide deaminases. We modified these highly conserved amino acids in the DYW motif of DYW1, an editing factor required for editing of the ndhD-1 site in Arabidopsis chloroplasts. We demonstrate that several amino acids of this signature motif are required for RNA editing in vivo and for zinc binding in vitro. We conclude that the DYW domain of DYW1 has features in common with cytidine deaminases, reinforcing the hypothesis that this domain forms part of the active enzyme that carries out RNA editing in plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25041347</PMID><DateCreated><Year>2014</Year><Month>08</Month><Day>01</Day></DateCreated><DateCompleted><Year>2015</Year><Month>04</Month><Day>03</Day></DateCompleted><DateRevised><Year>2014</Year><Month>08</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-8137</ISSN><JournalIssue CitedMedium="Internet"><Volume>203</Volume><Issue>4</Issue><PubDate><Year>2014</Year><Month>Sep</Month></PubDate></JournalIssue><Title>The New phytologist</Title><ISOAbbreviation>New Phytol.</ISOAbbreviation></Journal><ArticleTitle>The cytidine deaminase signature HxE(x)n CxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1.</ArticleTitle><Pagination><MedlinePgn>1090-5</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/nph.12928</ELocationID><Abstract><AbstractText>In flowering plants, RNA editing involves deamination of specific cytidines to uridines in both mitochondrial and chloroplast transcripts. Pentatricopeptide repeat (PPR) proteins and multiple organellar RNA editing factor (MORF) proteins have been shown to be involved in RNA editing but none have been shown to possess cytidine deaminase activity. The DYW domain of some PPR proteins contains a highly conserved signature resembling the zinc-binding active site motif of known nucleotide deaminases. We modified these highly conserved amino acids in the DYW motif of DYW1, an editing factor required for editing of the ndhD-1 site in Arabidopsis chloroplasts. We demonstrate that several amino acids of this signature motif are required for RNA editing in vivo and for zinc binding in vitro. We conclude that the DYW domain of DYW1 has features in common with cytidine deaminases, reinforcing the hypothesis that this domain forms part of the active enzyme that carries out RNA editing in plants.</AbstractText><CopyrightInformation>© 2014 The Authors. New Phytologist © 2014 New Phytologist Trust.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Boussardon</LastName><ForeName>Clément</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Unité de Recherche en Génomique Végétale (URGV), UMR INRA/UEVE - ERL CNRS, SPS Labex, CP 5708, 91057, Evry Cedex, France; Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, WA, 6009, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Avon</LastName><ForeName>Alexandra</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Kindgren</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Bond</LastName><ForeName>Charles S</ForeName><Initials>CS</Initials></Author><Author ValidYN="Y"><LastName>Challenor</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Lurin</LastName><ForeName>Claire</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Small</LastName><ForeName>Ian</ForeName><Initials>I</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>07</Month><Day>10</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="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C583235">DYW1 protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.5.4.5</RegistryNumber><NameOfSubstance UI="D003564">Cytidine Deaminase</NameOfSubstance></Chemical><Chemical><RegistryNumber>J41CSQ7QDS</RegistryNumber><NameOfSubstance UI="D015032">Zinc</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003564" MajorTopicYN="N">Cytidine Deaminase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017393" MajorTopicYN="N">RNA Editing</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013054" MajorTopicYN="N">Spectrophotometry, Atomic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040681" MajorTopicYN="N">Structural Homology, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">DYW domain</Keyword><Keyword MajorTopicYN="N">RNA editing</Keyword><Keyword MajorTopicYN="N">cytidine deaminase</Keyword><Keyword MajorTopicYN="N">pentatricopeptide repeat (PPR) proteins</Keyword><Keyword MajorTopicYN="N">zinc-binding motif</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>04</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>06</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25041347</ArticleId><ArticleId IdType="doi">10.1111/nph.12928</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Asie/explor/AustralieFrV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003466 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 003466 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Asie
|area= AustralieFrV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:25041347
|texte= The cytidine deaminase signature HxE(x)n CxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:25041347" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a AustralieFrV1
| This area was generated with Dilib version V0.6.33. |  |