Phosphoproteomics reveals extensive in vivo phosphorylation of Arabidopsis proteins involved in RNA metabolism
Identifieur interne : 001631 ( Main/Exploration ); précédent : 001630; suivant : 001632Phosphoproteomics reveals extensive in vivo phosphorylation of Arabidopsis proteins involved in RNA metabolism
Auteurs : Sergio De La Fuente Van Bentem ; Dorothea Anrather [Autriche] ; Elisabeth Roitinger [Autriche] ; Armin Djamei ; Thomas Hufnagl [Autriche] ; Andrea Barta [Autriche] ; Edina Csaszar [Autriche] ; Ilse Dohnal [Autriche] ; David Lecourieux ; Heribert HirtSource :
- Nucleic Acids Research [ 0305-1048 ] ; 2006.
Abstract
Most regulatory pathways are governed by the reversible phosphorylation of proteins. Recent developments in mass spectrometry-based technology allow the large-scale analysis of protein phosphorylation. Here, we show the application of immobilized metal affinity chromatography to purify phosphopeptides from Arabidopsis extracts. Phosphopeptide sequences were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS/MS). A total of 79 unique phosphorylation sites were determined in 22 phosphoproteins with a putative role in RNA metabolism, including splicing of mRNAs. Among these phosphoproteins, 12 Ser/Arg-rich (SR) splicing factors were identified. A conserved phosphorylation site was found in most of the phosphoproteins, including the SR proteins, suggesting that these proteins are targeted by the same or a highly related protein kinase. To test this hypothesis, Arabidopsis SR protein-specific kinase 4 (SRPK4) that was initially identified as an interactor of SR proteins was tested for its ability to phosphorylate the SR protein RSp31. In vitro kinase assays showed that all in vivo phosphorylation sites of RSp31 were targeted by SRPK4. These data suggest that the plant mRNA splicing machinery is a major target of phosphorylation and that a considerable number of proteins involved in RNA metabolism may be targeted by SRPKs.
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DOI: 10.1093/nar/gkl429
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Acids Res.</title><idno type="ISSN">0305-1048</idno><idno type="eISSN">1362-4962</idno><imprint><publisher>Oxford University Press</publisher><date type="published" when="2006">2006</date><biblScope unit="volume">34</biblScope><biblScope unit="issue">11</biblScope><biblScope unit="page" from="3267">3267</biblScope><biblScope unit="page" to="3278">3278</biblScope></imprint><idno type="ISSN">0305-1048</idno></series><idno type="istex">FA5262BCF890105EDC3908627BB54E02C75424B2</idno><idno type="DOI">10.1093/nar/gkl429</idno><idno type="local">gkl429</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0305-1048</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Most regulatory pathways are governed by the reversible phosphorylation of proteins. Recent developments in mass spectrometry-based technology allow the large-scale analysis of protein phosphorylation. Here, we show the application of immobilized metal affinity chromatography to purify phosphopeptides from Arabidopsis extracts. Phosphopeptide sequences were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS/MS). A total of 79 unique phosphorylation sites were determined in 22 phosphoproteins with a putative role in RNA metabolism, including splicing of mRNAs. Among these phosphoproteins, 12 Ser/Arg-rich (SR) splicing factors were identified. A conserved phosphorylation site was found in most of the phosphoproteins, including the SR proteins, suggesting that these proteins are targeted by the same or a highly related protein kinase. To test this hypothesis, Arabidopsis SR protein-specific kinase 4 (SRPK4) that was initially identified as an interactor of SR proteins was tested for its ability to phosphorylate the SR protein RSp31. In vitro kinase assays showed that all in vivo phosphorylation sites of RSp31 were targeted by SRPK4. These data suggest that the plant mRNA splicing machinery is a major target of phosphorylation and that a considerable number of proteins involved in RNA metabolism may be targeted by SRPKs.</div></front></TEI><affiliations><list><country><li>Autriche</li></country><region><li>Vienne (Autriche)</li></region><settlement><li>Vienne (Autriche)</li></settlement></list><tree><noCountry><name sortKey="Djamei, Armin" sort="Djamei, Armin" uniqKey="Djamei A" first="Armin" last="Djamei">Armin Djamei</name><name sortKey="Hirt, Heribert" sort="Hirt, Heribert" uniqKey="Hirt H" first="Heribert" last="Hirt">Heribert Hirt</name><name sortKey="Lecourieux, David" sort="Lecourieux, David" uniqKey="Lecourieux D" first="David" last="Lecourieux">David Lecourieux</name><name sortKey="Van Bentem, Sergio De La Fuente" sort="Van Bentem, Sergio De La Fuente" uniqKey="Van Bentem S" first="Sergio De La Fuente" last="Van Bentem">Sergio De La Fuente Van Bentem</name></noCountry><country name="Autriche"><region name="Vienne (Autriche)"><name sortKey="Anrather, Dorothea" sort="Anrather, Dorothea" uniqKey="Anrather D" first="Dorothea" last="Anrather">Dorothea Anrather</name></region><name sortKey="Barta, Andrea" sort="Barta, Andrea" uniqKey="Barta A" first="Andrea" last="Barta">Andrea Barta</name><name sortKey="Csaszar, Edina" sort="Csaszar, Edina" uniqKey="Csaszar E" first="Edina" last="Csaszar">Edina Csaszar</name><name sortKey="Dohnal, Ilse" sort="Dohnal, Ilse" uniqKey="Dohnal I" first="Ilse" last="Dohnal">Ilse Dohnal</name><name sortKey="Hufnagl, Thomas" sort="Hufnagl, Thomas" uniqKey="Hufnagl T" first="Thomas" last="Hufnagl">Thomas Hufnagl</name><name sortKey="Roitinger, Elisabeth" sort="Roitinger, Elisabeth" uniqKey="Roitinger E" first="Elisabeth" last="Roitinger">Elisabeth Roitinger</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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