The cytidine deaminase signature HxE(x)n CxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1.
Identifieur interne : 003444 ( Main/Exploration ); précédent : 003443; suivant : 003445The cytidine deaminase signature HxE(x)n CxxC of DYW1 binds zinc and is necessary for RNA editing of ndhD-1.
Auteurs : Clément Boussardon [Australie] ; Alexandra Avon ; Peter Kindgren ; Charles S. Bond ; Michael Challenor ; Claire Lurin ; Ian SmallSource :
- The New phytologist [ 1469-8137 ] ; 2014.
Descripteurs français
- KwdFr :
- Alignement de séquences, Arabidopsis (génétique), Cytidine deaminase (), Cytidine deaminase (métabolisme), Données de séquences moléculaires, Liaison aux protéines, Motifs d'acides aminés, Mutation (génétique), Protéines d'Arabidopsis (), Protéines d'Arabidopsis (métabolisme), Protéines de transport (), Protéines de transport (métabolisme), Relation structure-activité, Similitude structurale de protéines, Spectrophotométrie atomique, Structure tertiaire des protéines, Séquence d'acides aminés, Tryptophane (métabolisme), Zinc (métabolisme), Édition des ARN (génétique).
- MESH :
- génétique : Arabidopsis, Mutation, Édition des ARN.
- métabolisme : Cytidine deaminase, Protéines d'Arabidopsis, Protéines de transport, Tryptophane, Zinc.
- Alignement de séquences, Cytidine deaminase, Données de séquences moléculaires, Liaison aux protéines, Motifs d'acides aminés, Protéines d'Arabidopsis, Protéines de transport, Relation structure-activité, Similitude structurale de protéines, Spectrophotométrie atomique, Structure tertiaire des protéines, Séquence d'acides aminés.
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
Affiliations:
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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="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Arabidopsis (génétique)</term><term>Cytidine deaminase ()</term><term>Cytidine deaminase (métabolisme)</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Motifs d'acides aminés</term><term>Mutation (génétique)</term><term>Protéines d'Arabidopsis ()</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Protéines de transport ()</term><term>Protéines de transport (métabolisme)</term><term>Relation structure-activité</term><term>Similitude structurale de protéines</term><term>Spectrophotométrie atomique</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Tryptophane (métabolisme)</term><term>Zinc (métabolisme)</term><term>Édition des ARN (génétique)</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" qualifier="génétique" xml:lang="fr"><term>Arabidopsis</term><term>Mutation</term><term>Édition des ARN</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" qualifier="métabolisme" xml:lang="fr"><term>Cytidine deaminase</term><term>Protéines d'Arabidopsis</term><term>Protéines de transport</term><term>Tryptophane</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><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Cytidine deaminase</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Motifs d'acides aminés</term><term>Protéines d'Arabidopsis</term><term>Protéines de transport</term><term>Relation structure-activité</term><term>Similitude structurale de protéines</term><term>Spectrophotométrie atomique</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</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><affiliations><list><country><li>Australie</li></country></list><tree><noCountry><name sortKey="Avon, Alexandra" sort="Avon, Alexandra" uniqKey="Avon A" first="Alexandra" last="Avon">Alexandra Avon</name><name sortKey="Bond, Charles S" sort="Bond, Charles S" uniqKey="Bond C" first="Charles S" last="Bond">Charles S. Bond</name><name sortKey="Challenor, Michael" sort="Challenor, Michael" uniqKey="Challenor M" first="Michael" last="Challenor">Michael Challenor</name><name sortKey="Kindgren, Peter" sort="Kindgren, Peter" uniqKey="Kindgren P" first="Peter" last="Kindgren">Peter Kindgren</name><name sortKey="Lurin, Claire" sort="Lurin, Claire" uniqKey="Lurin C" first="Claire" last="Lurin">Claire Lurin</name><name sortKey="Small, Ian" sort="Small, Ian" uniqKey="Small I" first="Ian" last="Small">Ian Small</name></noCountry><country name="Australie"><noRegion><name sortKey="Boussardon, Clement" sort="Boussardon, Clement" uniqKey="Boussardon C" first="Clément" last="Boussardon">Clément Boussardon</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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