A receptor-like protein kinase with a lectin-like domain from lombardy poplar: gene expression in response to wounding and characterization of phosphorylation activity.
Identifieur interne : 004628 ( Main/Exploration ); précédent : 004627; suivant : 004629A receptor-like protein kinase with a lectin-like domain from lombardy poplar: gene expression in response to wounding and characterization of phosphorylation activity.
Auteurs : M. Nishiguchi [Japon] ; K. Yoshida ; T. Sumizono ; K. TazakiSource :
- Molecular genetics and genomics : MGG [ 1617-4615 ] ; 2002.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), ADN des plantes (génétique), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Gènes de plante (MeSH), Lectines (composition chimique), Lectines (génétique), Lectines végétales (MeSH), Maladies des plantes (génétique), Phosphorylation (MeSH), Protein kinases (composition chimique), Protein kinases (génétique), Protein kinases (métabolisme), Régulation de l'expression des gènes codant pour des enzymes (MeSH), Régulation de l'expression des gènes végétaux (MeSH), Salicaceae (enzymologie), Salicaceae (génétique), Similitude de séquences d'acides aminés (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Lectines, Protein kinases.
- enzymologie : Salicaceae.
- génétique : ADN complémentaire, ADN des plantes, Lectines, Maladies des plantes, Protein kinases, Salicaceae.
- métabolisme : Protein kinases.
- Clonage moléculaire, Données de séquences moléculaires, Gènes de plante, Lectines végétales, Phosphorylation, Régulation de l'expression des gènes codant pour des enzymes, Régulation de l'expression des gènes végétaux, Similitude de séquences d'acides aminés, Structure tertiaire des protéines, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), DNA, Complementary (genetics), DNA, Plant (genetics), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), Genes, Plant (MeSH), Lectins (chemistry), Lectins (genetics), Molecular Sequence Data (MeSH), Phosphorylation (MeSH), Plant Diseases (genetics), Plant Lectins (MeSH), Protein Kinases (chemistry), Protein Kinases (genetics), Protein Kinases (metabolism), Protein Structure, Tertiary (MeSH), Salicaceae (enzymology), Salicaceae (genetics), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Lectins, Protein Kinases.
- chemical , genetics : DNA, Complementary, DNA, Plant, Lectins, Protein Kinases.
- enzymology : Salicaceae.
- genetics : Plant Diseases, Salicaceae.
- chemical , metabolism : Protein Kinases.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Genes, Plant, Molecular Sequence Data, Phosphorylation, Plant Lectins, Protein Structure, Tertiary, Sequence Homology, Amino Acid.
Abstract
Plant receptor-like protein kinases (RLKs) are thought to be involved in various cellular processes mediated via signal transduction pathways. To clarify the initial step in such a signal transduction pathway in woody plants, we cloned a cDNA encoding PnLPK (a P opulus n igra var. italica lectin-like protein kinase) from lombardy poplar. The C-terminal region of the predicted PnLPK protein includes a protein kinase catalytic domain consisting of the 12 subdomains typical of the eukaryotic protein kinase superfamily. Following the signal peptide at the N-terminus, a domain that shows homology to legume lectins retains the putative Mn(2+)- and Ca(2+)-binding amino acids, which are highly conserved among lectin-related proteins. Because a putative hydrophobic transmembrane domain was localized between the lectin-like domain and the protein kinase domain, PnLPK was determined to be a member of the plant RLK subfamily with a lectin-like domain. Transcripts of the PnLPK gene accumulate in roots, mature leaves and calli of lombardy poplar, whereas only trace amounts of the transcripts are detectable in stems, young leaves and apical buds. Wounding of the young leaves increased the amount of PnLPK mRNA, but none of several phytohormones tested had any effect on the transcription of PnLPK. When incubated in the presence of divalent metal cations such as Mn(2+), the C-terminal catalytic domain of PnLPK showed significantly higher autophosphorylation activity than the full-length PnLPK protein. The phosphorylation activity of PnLPK was also detected using beta-casein as substrate. Phosphoamino acid analysis indicated that PnLPK is a serine/threonine kinase.
DOI: 10.1007/s00438-002-0683-4
PubMed: 12111558
Affiliations:
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Tazaki</name></author></analytic><series><title level="j">Molecular genetics and genomics : MGG</title><idno type="ISSN">1617-4615</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>DNA, Complementary (genetics)</term><term>DNA, Plant (genetics)</term><term>Gene Expression Regulation, Enzymologic (MeSH)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Genes, Plant (MeSH)</term><term>Lectins (chemistry)</term><term>Lectins (genetics)</term><term>Molecular Sequence Data (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Plant Diseases (genetics)</term><term>Plant Lectins (MeSH)</term><term>Protein Kinases (chemistry)</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (metabolism)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Salicaceae (enzymology)</term><term>Salicaceae (genetics)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (génétique)</term><term>ADN des plantes (génétique)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Gènes de plante (MeSH)</term><term>Lectines (composition chimique)</term><term>Lectines (génétique)</term><term>Lectines végétales (MeSH)</term><term>Maladies des plantes (génétique)</term><term>Phosphorylation (MeSH)</term><term>Protein kinases (composition chimique)</term><term>Protein kinases (génétique)</term><term>Protein kinases (métabolisme)</term><term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Salicaceae (enzymologie)</term><term>Salicaceae (génétique)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lectins</term><term>Protein Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Complementary</term><term>DNA, Plant</term><term>Lectins</term><term>Protein Kinases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Lectines</term><term>Protein kinases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Salicaceae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Salicaceae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Plant Diseases</term><term>Salicaceae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN complémentaire</term><term>ADN des plantes</term><term>Lectines</term><term>Maladies des plantes</term><term>Protein kinases</term><term>Salicaceae</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protein Kinases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protein kinases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Gene Expression Regulation, Enzymologic</term><term>Gene Expression Regulation, Plant</term><term>Genes, Plant</term><term>Molecular Sequence Data</term><term>Phosphorylation</term><term>Plant Lectins</term><term>Protein Structure, Tertiary</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Gènes de plante</term><term>Lectines végétales</term><term>Phosphorylation</term><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Régulation de l'expression des gènes végétaux</term><term>Similitude de séquences d'acides aminés</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plant receptor-like protein kinases (RLKs) are thought to be involved in various cellular processes mediated via signal transduction pathways. To clarify the initial step in such a signal transduction pathway in woody plants, we cloned a cDNA encoding PnLPK (a P opulus n igra var. italica lectin-like protein kinase) from lombardy poplar. The C-terminal region of the predicted PnLPK protein includes a protein kinase catalytic domain consisting of the 12 subdomains typical of the eukaryotic protein kinase superfamily. Following the signal peptide at the N-terminus, a domain that shows homology to legume lectins retains the putative Mn(2+)- and Ca(2+)-binding amino acids, which are highly conserved among lectin-related proteins. Because a putative hydrophobic transmembrane domain was localized between the lectin-like domain and the protein kinase domain, PnLPK was determined to be a member of the plant RLK subfamily with a lectin-like domain. Transcripts of the PnLPK gene accumulate in roots, mature leaves and calli of lombardy poplar, whereas only trace amounts of the transcripts are detectable in stems, young leaves and apical buds. Wounding of the young leaves increased the amount of PnLPK mRNA, but none of several phytohormones tested had any effect on the transcription of PnLPK. When incubated in the presence of divalent metal cations such as Mn(2+), the C-terminal catalytic domain of PnLPK showed significantly higher autophosphorylation activity than the full-length PnLPK protein. The phosphorylation activity of PnLPK was also detected using beta-casein as substrate. Phosphoamino acid analysis indicated that PnLPK is a serine/threonine kinase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12111558</PMID><DateCompleted><Year>2002</Year><Month>08</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1617-4615</ISSN><JournalIssue CitedMedium="Print"><Volume>267</Volume><Issue>4</Issue><PubDate><Year>2002</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Molecular genetics and genomics : MGG</Title><ISOAbbreviation>Mol Genet Genomics</ISOAbbreviation></Journal><ArticleTitle>A receptor-like protein kinase with a lectin-like domain from lombardy poplar: gene expression in response to wounding and characterization of phosphorylation activity.</ArticleTitle><Pagination><MedlinePgn>506-14</MedlinePgn></Pagination><Abstract><AbstractText>Plant receptor-like protein kinases (RLKs) are thought to be involved in various cellular processes mediated via signal transduction pathways. To clarify the initial step in such a signal transduction pathway in woody plants, we cloned a cDNA encoding PnLPK (a P opulus n igra var. italica lectin-like protein kinase) from lombardy poplar. The C-terminal region of the predicted PnLPK protein includes a protein kinase catalytic domain consisting of the 12 subdomains typical of the eukaryotic protein kinase superfamily. Following the signal peptide at the N-terminus, a domain that shows homology to legume lectins retains the putative Mn(2+)- and Ca(2+)-binding amino acids, which are highly conserved among lectin-related proteins. Because a putative hydrophobic transmembrane domain was localized between the lectin-like domain and the protein kinase domain, PnLPK was determined to be a member of the plant RLK subfamily with a lectin-like domain. Transcripts of the PnLPK gene accumulate in roots, mature leaves and calli of lombardy poplar, whereas only trace amounts of the transcripts are detectable in stems, young leaves and apical buds. Wounding of the young leaves increased the amount of PnLPK mRNA, but none of several phytohormones tested had any effect on the transcription of PnLPK. When incubated in the presence of divalent metal cations such as Mn(2+), the C-terminal catalytic domain of PnLPK showed significantly higher autophosphorylation activity than the full-length PnLPK protein. The phosphorylation activity of PnLPK was also detected using beta-casein as substrate. Phosphoamino acid analysis indicated that PnLPK is a serine/threonine kinase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nishiguchi</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Forestry and Forest Products Research Institute, Kukizaki, Ibaraki 305-8687, Japan. nishi3@ffpri.affrc.go.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yoshida</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Sumizono</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Tazaki</LastName><ForeName>K</ForeName><Initials>K</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>2002</Year><Month>05</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Mol Genet Genomics</MedlineTA><NlmUniqueID>101093320</NlmUniqueID><ISSNLinking>1617-4623</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018744">DNA, Plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037102">Lectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037121">Plant Lectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018744" MajorTopicYN="N">DNA, Plant</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017343" MajorTopicYN="Y">Genes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037102" MajorTopicYN="N">Lectins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D037121" MajorTopicYN="N">Plant Lectins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D031308" MajorTopicYN="N">Salicaceae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2002</Year><Month>04</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2002</Year><Month>04</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>7</Month><Day>12</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>8</Month><Day>16</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>7</Month><Day>12</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12111558</ArticleId><ArticleId IdType="doi">10.1007/s00438-002-0683-4</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Sumizono, T" sort="Sumizono, T" uniqKey="Sumizono T" first="T" last="Sumizono">T. Sumizono</name><name sortKey="Tazaki, K" sort="Tazaki, K" uniqKey="Tazaki K" first="K" last="Tazaki">K. Tazaki</name><name sortKey="Yoshida, K" sort="Yoshida, K" uniqKey="Yoshida K" first="K" last="Yoshida">K. Yoshida</name></noCountry><country name="Japon"><noRegion><name sortKey="Nishiguchi, M" sort="Nishiguchi, M" uniqKey="Nishiguchi M" first="M" last="Nishiguchi">M. Nishiguchi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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