Phosphoproteomic identification and phylogenetic analysis of ribosomal P-proteins in Populus dormant terminal buds.
Identifieur interne : 003170 ( Main/Exploration ); précédent : 003169; suivant : 003171Phosphoproteomic identification and phylogenetic analysis of ribosomal P-proteins in Populus dormant terminal buds.
Auteurs : Chang-Cai Liu [République populaire de Chine] ; Tian-Cong Lu ; Hua-Hua Li ; Hong-Xia Wang ; Gui-Feng Liu ; Ling Ma ; Chuan-Ping Yang ; Bai-Chen WangSource :
- Planta [ 1432-2048 ] ; 2010.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Analyse de séquence de protéine (MeSH), Données de séquences moléculaires (MeSH), Phosphoprotéines (composition chimique), Phosphoprotéines (génétique), Phosphorylation (MeSH), Phylogenèse (MeSH), Populus (génétique), Populus (métabolisme), Protéines ribosomiques (composition chimique), Protéines ribosomiques (génétique), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéomique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Phosphoprotéines, Protéines ribosomiques, Protéines végétales.
- génétique : Phosphoprotéines, Populus, Protéines ribosomiques, Protéines végétales.
- métabolisme : Populus.
- Alignement de séquences, Analyse de séquence de protéine, Données de séquences moléculaires, Phosphorylation, Phylogenèse, Protéomique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Molecular Sequence Data (MeSH), Phosphoproteins (chemistry), Phosphoproteins (genetics), Phosphorylation (MeSH), Phylogeny (MeSH), Plant Proteins (chemistry), Plant Proteins (genetics), Populus (genetics), Populus (metabolism), Proteomics (MeSH), Ribosomal Proteins (chemistry), Ribosomal Proteins (genetics), Sequence Alignment (MeSH), Sequence Analysis, Protein (MeSH).
- MESH :
- chemical , chemistry : Phosphoproteins, Plant Proteins, Ribosomal Proteins.
- chemical , genetics : Phosphoproteins, Plant Proteins, Ribosomal Proteins.
- genetics : Populus.
- metabolism : Populus.
- Amino Acid Sequence, Molecular Sequence Data, Phosphorylation, Phylogeny, Proteomics, Sequence Alignment, Sequence Analysis, Protein.
Abstract
To better understand the role that reversible phosphorylation plays in woody plant ribosomal P-protein function, we initiated a phosphoproteomic investigation of P-proteins from Populus dormant terminal buds. Using gel-free (in-solution) protein digestion and phosphopeptide enrichment combined with a nanoUPLC-ESI-MS/MS strategy, we identified six phosphorylation sites on eight P-proteins from Populus dormant terminal buds. Among these, six Ser sites and one Thr site were identified in the highly conserved C-terminal region of eight P-proteins of various P-protein subfamilies, including two P0, two P1, three P2 and one P3 protein. Among these, the Thr site was shown to be novel and has not been identified in any other organisms. Sequence analysis indicated that the phosphothreonine sites identified in the C-terminus of Ptr RPP2A exclusively occurred in woody species of Populus, etc. The identified phosphopeptides shared a common phosphorylation motif of (S/T)XX(D/E) and may be phosphorylated in vivo by casein kinase 2 as suggested by using Scansite analysis. Furthermore, phylogenetic analysis suggested that divergence of P2 also occurred in Populus, including type I and type II. To the best of our knowledge, this is the first systematic phosphoproteomic and phylogenetic analysis of P-proteins in woody plants, the results of which will provide a wealth of resources for future understanding and unraveling of the regulatory mechanisms of Populus P-protein phosphorylation during the maintenance of dormancy.
DOI: 10.1007/s00425-009-1037-9
PubMed: 20072825
Affiliations:
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last="Yang">Chuan-Ping Yang</name></author><author><name sortKey="Wang, Bai Chen" sort="Wang, Bai Chen" uniqKey="Wang B" first="Bai-Chen" last="Wang">Bai-Chen Wang</name></author></analytic><series><title level="j">Planta</title><idno type="eISSN">1432-2048</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phosphoproteins (chemistry)</term><term>Phosphoproteins (genetics)</term><term>Phosphorylation (MeSH)</term><term>Phylogeny (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Populus (genetics)</term><term>Populus (metabolism)</term><term>Proteomics (MeSH)</term><term>Ribosomal Proteins (chemistry)</term><term>Ribosomal Proteins (genetics)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Analysis, Protein (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Analyse de séquence de protéine (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Phosphoprotéines (composition chimique)</term><term>Phosphoprotéines (génétique)</term><term>Phosphorylation (MeSH)</term><term>Phylogenèse (MeSH)</term><term>Populus (génétique)</term><term>Populus (métabolisme)</term><term>Protéines ribosomiques (composition chimique)</term><term>Protéines ribosomiques (génétique)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (génétique)</term><term>Protéomique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Phosphoproteins</term><term>Plant Proteins</term><term>Ribosomal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Phosphoproteins</term><term>Plant Proteins</term><term>Ribosomal Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Phosphoprotéines</term><term>Protéines ribosomiques</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phosphoprotéines</term><term>Populus</term><term>Protéines ribosomiques</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Molecular Sequence Data</term><term>Phosphorylation</term><term>Phylogeny</term><term>Proteomics</term><term>Sequence Alignment</term><term>Sequence Analysis, Protein</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Analyse de séquence de protéine</term><term>Données de séquences moléculaires</term><term>Phosphorylation</term><term>Phylogenèse</term><term>Protéomique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To better understand the role that reversible phosphorylation plays in woody plant ribosomal P-protein function, we initiated a phosphoproteomic investigation of P-proteins from Populus dormant terminal buds. Using gel-free (in-solution) protein digestion and phosphopeptide enrichment combined with a nanoUPLC-ESI-MS/MS strategy, we identified six phosphorylation sites on eight P-proteins from Populus dormant terminal buds. Among these, six Ser sites and one Thr site were identified in the highly conserved C-terminal region of eight P-proteins of various P-protein subfamilies, including two P0, two P1, three P2 and one P3 protein. Among these, the Thr site was shown to be novel and has not been identified in any other organisms. Sequence analysis indicated that the phosphothreonine sites identified in the C-terminus of Ptr RPP2A exclusively occurred in woody species of Populus, etc. The identified phosphopeptides shared a common phosphorylation motif of (S/T)XX(D/E) and may be phosphorylated in vivo by casein kinase 2 as suggested by using Scansite analysis. Furthermore, phylogenetic analysis suggested that divergence of P2 also occurred in Populus, including type I and type II. To the best of our knowledge, this is the first systematic phosphoproteomic and phylogenetic analysis of P-proteins in woody plants, the results of which will provide a wealth of resources for future understanding and unraveling of the regulatory mechanisms of Populus P-protein phosphorylation during the maintenance of dormancy.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20072825</PMID><DateCompleted><Year>2010</Year><Month>07</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-2048</ISSN><JournalIssue CitedMedium="Internet"><Volume>231</Volume><Issue>3</Issue><PubDate><Year>2010</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Phosphoproteomic identification and phylogenetic analysis of ribosomal P-proteins in Populus dormant terminal buds.</ArticleTitle><Pagination><MedlinePgn>571-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00425-009-1037-9</ELocationID><Abstract><AbstractText>To better understand the role that reversible phosphorylation plays in woody plant ribosomal P-protein function, we initiated a phosphoproteomic investigation of P-proteins from Populus dormant terminal buds. Using gel-free (in-solution) protein digestion and phosphopeptide enrichment combined with a nanoUPLC-ESI-MS/MS strategy, we identified six phosphorylation sites on eight P-proteins from Populus dormant terminal buds. Among these, six Ser sites and one Thr site were identified in the highly conserved C-terminal region of eight P-proteins of various P-protein subfamilies, including two P0, two P1, three P2 and one P3 protein. Among these, the Thr site was shown to be novel and has not been identified in any other organisms. Sequence analysis indicated that the phosphothreonine sites identified in the C-terminus of Ptr RPP2A exclusively occurred in woody species of Populus, etc. The identified phosphopeptides shared a common phosphorylation motif of (S/T)XX(D/E) and may be phosphorylated in vivo by casein kinase 2 as suggested by using Scansite analysis. Furthermore, phylogenetic analysis suggested that divergence of P2 also occurred in Populus, including type I and type II. To the best of our knowledge, this is the first systematic phosphoproteomic and phylogenetic analysis of P-proteins in woody plants, the results of which will provide a wealth of resources for future understanding and unraveling of the regulatory mechanisms of Populus P-protein phosphorylation during the maintenance of dormancy.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Chang-Cai</ForeName><Initials>CC</Initials><AffiliationInfo><Affiliation>Education Ministry Key Laboratory of Forest Tree Genetic Improvement and Biotechnology, Northeast Forestry University, 26 Hexing Road, 150040 Harbin, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Tian-Cong</ForeName><Initials>TC</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Hua-Hua</ForeName><Initials>HH</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Hong-Xia</ForeName><Initials>HX</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Gui-Feng</ForeName><Initials>GF</Initials></Author><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Ling</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Chuan-Ping</ForeName><Initials>CP</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Bai-Chen</ForeName><Initials>BC</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 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MajorTopicYN="N">Phosphoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="Y">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040901" 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de Chine</li></country></list><tree><noCountry><name sortKey="Li, Hua Hua" sort="Li, Hua Hua" uniqKey="Li H" first="Hua-Hua" last="Li">Hua-Hua Li</name><name sortKey="Liu, Gui Feng" sort="Liu, Gui Feng" uniqKey="Liu G" first="Gui-Feng" last="Liu">Gui-Feng Liu</name><name sortKey="Lu, Tian Cong" sort="Lu, Tian Cong" uniqKey="Lu T" first="Tian-Cong" last="Lu">Tian-Cong Lu</name><name sortKey="Ma, Ling" sort="Ma, Ling" uniqKey="Ma L" first="Ling" last="Ma">Ling Ma</name><name sortKey="Wang, Bai Chen" sort="Wang, Bai Chen" uniqKey="Wang B" first="Bai-Chen" last="Wang">Bai-Chen Wang</name><name sortKey="Wang, Hong Xia" sort="Wang, Hong Xia" uniqKey="Wang H" first="Hong-Xia" last="Wang">Hong-Xia Wang</name><name sortKey="Yang, Chuan Ping" sort="Yang, Chuan Ping" uniqKey="Yang C" first="Chuan-Ping" last="Yang">Chuan-Ping Yang</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Liu, Chang Cai" sort="Liu, Chang Cai" uniqKey="Liu C" first="Chang-Cai" last="Liu">Chang-Cai Liu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Phosphoproteomic identification and phylogenetic analysis of ribosomal P-proteins in Populus dormant terminal buds.
}}
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