Quantitative label-free phosphoproteomics of six different life stages of the late blight pathogen Phytophthora infestans reveals abundant phosphorylation of members of the CRN effector family.
Identifieur interne : 001000 ( Main/Exploration ); précédent : 000F99; suivant : 001001Quantitative label-free phosphoproteomics of six different life stages of the late blight pathogen Phytophthora infestans reveals abundant phosphorylation of members of the CRN effector family.
Auteurs : Svante Resjö [Suède] ; Ashfaq Ali ; Harold J G. Meijer ; Michael F. Seidl ; Berend Snel ; Marianne Sandin ; Fredrik Levander ; Francine Govers ; Erik AndreassonSource :
- Journal of proteome research [ 1535-3907 ] ; 2014.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires (MeSH), Motifs d'acides aminés (MeSH), Phosphopeptides (analyse), Phosphopeptides (composition chimique), Phosphopeptides (métabolisme), Phosphoprotéines (analyse), Phosphoprotéines (composition chimique), Phosphoprotéines (métabolisme), Phosphorylation (MeSH), Phytophthora infestans (composition chimique), Phytophthora infestans (métabolisme), Phytophthora infestans (physiologie), Protein-Serine-Threonine Kinases (analyse), Protein-Serine-Threonine Kinases (composition chimique), Protein-Serine-Threonine Kinases (métabolisme), Protéomique (MeSH), Séquence d'acides aminés (MeSH), Techniques de culture de tissus (MeSH), Étapes du cycle de vie (physiologie).
- MESH :
- analyse : Phosphopeptides, Phosphoprotéines, Protein-Serine-Threonine Kinases.
- composition chimique : Phosphopeptides, Phosphoprotéines, Phytophthora infestans, Protein-Serine-Threonine Kinases.
- métabolisme : Phosphopeptides, Phosphoprotéines, Phytophthora infestans, Protein-Serine-Threonine Kinases.
- physiologie : Phytophthora infestans, Étapes du cycle de vie.
- Données de séquences moléculaires, Motifs d'acides aminés, Phosphorylation, Protéomique, Séquence d'acides aminés, Techniques de culture de tissus.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Life Cycle Stages (physiology), Molecular Sequence Data (MeSH), Phosphopeptides (analysis), Phosphopeptides (chemistry), Phosphopeptides (metabolism), Phosphoproteins (analysis), Phosphoproteins (chemistry), Phosphoproteins (metabolism), Phosphorylation (MeSH), Phytophthora infestans (chemistry), Phytophthora infestans (metabolism), Phytophthora infestans (physiology), Protein-Serine-Threonine Kinases (analysis), Protein-Serine-Threonine Kinases (chemistry), Protein-Serine-Threonine Kinases (metabolism), Proteomics (MeSH), Tissue Culture Techniques (MeSH).
- MESH :
- chemical , analysis : Phosphopeptides, Phosphoproteins, Protein-Serine-Threonine Kinases.
- chemical , chemistry : Phosphopeptides, Phosphoproteins, Protein-Serine-Threonine Kinases.
- chemical , metabolism : Phosphopeptides, Phosphoproteins, Protein-Serine-Threonine Kinases.
- chemistry : Phytophthora infestans.
- metabolism : Phytophthora infestans.
- physiology : Life Cycle Stages, Phytophthora infestans.
- Amino Acid Motifs, Amino Acid Sequence, Molecular Sequence Data, Phosphorylation, Proteomics, Tissue Culture Techniques.
Abstract
The oomycete Phytophthora infestans is the causal agent of late blight in potato and tomato. Since the underlying processes that govern pathogenicity and development in P. infestans are largely unknown, we have performed a large-scale phosphoproteomics study of six different P. infestans life stages. We have obtained quantitative data for 2922 phosphopeptides and compared their abundance. Life-stage-specific phosphopeptides include ATP-binding cassette transporters and a kinase that only occurs in appressoria. In an extended data set, we identified 2179 phosphorylation sites and deduced 22 phosphomotifs. Several of the phosphomotifs matched consensus sequences of kinases that occur in P. infestans but not Arabidopsis. In addition, we detected tyrosine phosphopeptides that are potential targets of kinases resembling mammalian tyrosine kinases. Among the phosphorylated proteins are members of the RXLR and Crinkler effector families. The latter are phosphorylated in several life stages and at multiple positions, in sites that are conserved between different members of the Crinkler family. This indicates that proteins in the Crinkler family have functions beyond their putative role as (necrosis-inducing) effectors. This phosphoproteomics data will be instrumental for studies on oomycetes and host-oomycete interactions. The data sets have been deposited to ProteomeXchange (identifier PXD000433).
DOI: 10.1021/pr4009095
PubMed: 24588563
Affiliations:
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scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Life Cycle Stages (physiology)</term><term>Molecular Sequence Data (MeSH)</term><term>Phosphopeptides (analysis)</term><term>Phosphopeptides (chemistry)</term><term>Phosphopeptides (metabolism)</term><term>Phosphoproteins (analysis)</term><term>Phosphoproteins (chemistry)</term><term>Phosphoproteins (metabolism)</term><term>Phosphorylation (MeSH)</term><term>Phytophthora infestans (chemistry)</term><term>Phytophthora infestans (metabolism)</term><term>Phytophthora infestans (physiology)</term><term>Protein-Serine-Threonine Kinases (analysis)</term><term>Protein-Serine-Threonine Kinases (chemistry)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Proteomics (MeSH)</term><term>Tissue Culture Techniques (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Phosphopeptides (analyse)</term><term>Phosphopeptides (composition chimique)</term><term>Phosphopeptides (métabolisme)</term><term>Phosphoprotéines (analyse)</term><term>Phosphoprotéines (composition chimique)</term><term>Phosphoprotéines (métabolisme)</term><term>Phosphorylation (MeSH)</term><term>Phytophthora infestans (composition chimique)</term><term>Phytophthora infestans (métabolisme)</term><term>Phytophthora infestans (physiologie)</term><term>Protein-Serine-Threonine Kinases (analyse)</term><term>Protein-Serine-Threonine Kinases (composition chimique)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéomique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Techniques de culture de tissus (MeSH)</term><term>Étapes du cycle de vie (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Phosphopeptides</term><term>Phosphoproteins</term><term>Protein-Serine-Threonine 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infestans</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phosphopeptides</term><term>Phosphoprotéines</term><term>Phytophthora infestans</term><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Phytophthora infestans</term><term>Étapes du cycle de vie</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Life Cycle Stages</term><term>Phytophthora infestans</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Phosphorylation</term><term>Proteomics</term><term>Tissue Culture Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Motifs d'acides aminés</term><term>Phosphorylation</term><term>Protéomique</term><term>Séquence d'acides aminés</term><term>Techniques de culture de tissus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The oomycete Phytophthora infestans is the causal agent of late blight in potato and tomato. Since the underlying processes that govern pathogenicity and development in P. infestans are largely unknown, we have performed a large-scale phosphoproteomics study of six different P. infestans life stages. We have obtained quantitative data for 2922 phosphopeptides and compared their abundance. Life-stage-specific phosphopeptides include ATP-binding cassette transporters and a kinase that only occurs in appressoria. In an extended data set, we identified 2179 phosphorylation sites and deduced 22 phosphomotifs. Several of the phosphomotifs matched consensus sequences of kinases that occur in P. infestans but not Arabidopsis. In addition, we detected tyrosine phosphopeptides that are potential targets of kinases resembling mammalian tyrosine kinases. Among the phosphorylated proteins are members of the RXLR and Crinkler effector families. The latter are phosphorylated in several life stages and at multiple positions, in sites that are conserved between different members of the Crinkler family. This indicates that proteins in the Crinkler family have functions beyond their putative role as (necrosis-inducing) effectors. This phosphoproteomics data will be instrumental for studies on oomycetes and host-oomycete interactions. The data sets have been deposited to ProteomeXchange (identifier PXD000433). </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24588563</PMID><DateCompleted><Year>2014</Year><Month>12</Month><Day>08</Day></DateCompleted><DateRevised><Year>2014</Year><Month>04</Month><Day>04</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1535-3907</ISSN><JournalIssue CitedMedium="Internet"><Volume>13</Volume><Issue>4</Issue><PubDate><Year>2014</Year><Month>Apr</Month><Day>04</Day></PubDate></JournalIssue><Title>Journal of proteome research</Title><ISOAbbreviation>J Proteome Res</ISOAbbreviation></Journal><ArticleTitle>Quantitative label-free phosphoproteomics of six different life stages of the late blight pathogen Phytophthora infestans reveals abundant phosphorylation of members of the CRN effector family.</ArticleTitle><Pagination><MedlinePgn>1848-59</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/pr4009095</ELocationID><Abstract><AbstractText>The oomycete Phytophthora infestans is the causal agent of late blight in potato and tomato. Since the underlying processes that govern pathogenicity and development in P. infestans are largely unknown, we have performed a large-scale phosphoproteomics study of six different P. infestans life stages. We have obtained quantitative data for 2922 phosphopeptides and compared their abundance. Life-stage-specific phosphopeptides include ATP-binding cassette transporters and a kinase that only occurs in appressoria. In an extended data set, we identified 2179 phosphorylation sites and deduced 22 phosphomotifs. Several of the phosphomotifs matched consensus sequences of kinases that occur in P. infestans but not Arabidopsis. In addition, we detected tyrosine phosphopeptides that are potential targets of kinases resembling mammalian tyrosine kinases. Among the phosphorylated proteins are members of the RXLR and Crinkler effector families. The latter are phosphorylated in several life stages and at multiple positions, in sites that are conserved between different members of the Crinkler family. This indicates that proteins in the Crinkler family have functions beyond their putative role as (necrosis-inducing) effectors. This phosphoproteomics data will be instrumental for studies on oomycetes and host-oomycete interactions. The data sets have been deposited to ProteomeXchange (identifier PXD000433). </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Resjö</LastName><ForeName>Svante</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Plant Protection Biology, Swedish University of Agricultural Sciences , SE-230 53 Alnarp, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ali</LastName><ForeName>Ashfaq</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Meijer</LastName><ForeName>Harold J G</ForeName><Initials>HJ</Initials></Author><Author ValidYN="Y"><LastName>Seidl</LastName><ForeName>Michael F</ForeName><Initials>MF</Initials></Author><Author ValidYN="Y"><LastName>Snel</LastName><ForeName>Berend</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Sandin</LastName><ForeName>Marianne</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Levander</LastName><ForeName>Fredrik</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Govers</LastName><ForeName>Francine</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Andreasson</LastName><ForeName>Erik</ForeName><Initials>E</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>03</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Proteome Res</MedlineTA><NlmUniqueID>101128775</NlmUniqueID><ISSNLinking>1535-3893</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010748">Phosphopeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010750">Phosphoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</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="D008018" MajorTopicYN="N">Life Cycle Stages</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010748" MajorTopicYN="N">Phosphopeptides</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055750" MajorTopicYN="N">Phytophthora infestans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046509" MajorTopicYN="N">Tissue Culture Techniques</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>3</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>3</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24588563</ArticleId><ArticleId IdType="doi">10.1021/pr4009095</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Ali, Ashfaq" sort="Ali, Ashfaq" uniqKey="Ali A" first="Ashfaq" last="Ali">Ashfaq Ali</name><name sortKey="Andreasson, Erik" sort="Andreasson, Erik" uniqKey="Andreasson E" first="Erik" last="Andreasson">Erik Andreasson</name><name sortKey="Govers, Francine" sort="Govers, Francine" uniqKey="Govers F" first="Francine" last="Govers">Francine Govers</name><name sortKey="Levander, Fredrik" sort="Levander, Fredrik" uniqKey="Levander F" first="Fredrik" last="Levander">Fredrik Levander</name><name sortKey="Meijer, Harold J G" sort="Meijer, Harold J G" uniqKey="Meijer H" first="Harold J G" last="Meijer">Harold J G. Meijer</name><name sortKey="Sandin, Marianne" sort="Sandin, Marianne" uniqKey="Sandin M" first="Marianne" last="Sandin">Marianne Sandin</name><name sortKey="Seidl, Michael F" sort="Seidl, Michael F" uniqKey="Seidl M" first="Michael F" last="Seidl">Michael F. Seidl</name><name sortKey="Snel, Berend" sort="Snel, Berend" uniqKey="Snel B" first="Berend" last="Snel">Berend Snel</name></noCountry><country name="Suède"><noRegion><name sortKey="Resjo, Svante" sort="Resjo, Svante" uniqKey="Resjo S" first="Svante" last="Resjö">Svante Resjö</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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