PoplarV1, Main, Exploration, bibRecord, 004041

Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.

Identifieur interne : 004041 ( Main/Exploration ); précédent : 004040; suivant : 004042

Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.

Auteurs : Sabine André [Allemagne] ; Hans-Christian Siebert ; Mitsuru Nishiguchi ; Kiyoshi Tazaki ; Hans-Joachim Gabius

Source :

Biochimica et biophysica acta [ 0006-3002 ] ; 2005.

RBID : pubmed:15878637

Descripteurs français

English descriptors

KwdEn :
- Algorithms (MeSH), Amino Acid Sequence (MeSH), Binding Sites (MeSH), Computational Biology (methods), Computer Simulation (MeSH), Conserved Sequence (MeSH), Enzyme Activation (MeSH), Glycoproteins (analysis), Glycoproteins (chemistry), Models, Chemical (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Plant Lectins (analysis), Plant Lectins (chemistry), Plant Proteins (analysis), Plant Proteins (chemistry), Populus (enzymology), Protein Binding (MeSH), Protein-Serine-Threonine Kinases (analysis), Protein-Serine-Threonine Kinases (chemistry), Receptors, Cell Surface (analysis), Receptors, Cell Surface (chemistry), Sequence Alignment (methods), Sequence Analysis, Protein (methods), Sequence Homology, Amino Acid (MeSH).
MESH :
- chemical , analysis : Glycoproteins, Plant Lectins, Plant Proteins, Protein-Serine-Threonine Kinases, Receptors, Cell Surface.
- chemical , chemistry : Glycoproteins, Plant Lectins, Plant Proteins, Protein-Serine-Threonine Kinases, Receptors, Cell Surface.
- enzymology : Populus.
- methods : Computational Biology, Sequence Alignment, Sequence Analysis, Protein.
- Algorithms, Amino Acid Sequence, Binding Sites, Computer Simulation, Conserved Sequence, Enzyme Activation, Models, Chemical, Models, Molecular, Molecular Sequence Data, Protein Binding, Sequence Homology, Amino Acid.

Abstract

Detection of genes for putative receptor-like protein kinases, which contain an extracellular domain related to leguminous lectins, in plant genomes inspired the hypothesis that this part acts as sensor. Initial support for this concept came from proof for protein kinase activity. The next step, focusing on the protein of lombardy poplar (Populus nigra var. italica), is scrutiny for lectin activity. Consequently, we first pinpointed sets of high-scoring sequence pairs by extensive databank search. The calculations resulted in P-values in the range from 10(-14) to 10(-18) exclusively for leguminous lectins, the Pterocarpus angolensis agglutinin being front runner with P=3 x 10(-18) and thus most suitable template for modeling. The superimposition of the two folds gave notable similarity in the region responsible for binding carbohydrate and Ca(2+)/Mn(2+)-ions. Binding activity toward carbohydrates was detected by assaying a panel of (neo)glycoproteins as polyvalent probes, especially for alpha-l-rhamnose and glycans of asialofetuin. It was strictly dependent on Ca(2+)-ions, enhanced by Mn(2+)-ions and reached a K(D)-value of 34.3 nM for the neoglycoprotein with rhamnose as ligand. These results give further research direction to define physiological ligands, plant/bacterial rhamnose-containing saccharides and rhamnose-mimetic glycans or peptides being potential candidates.

DOI: 10.1016/j.bbagen.2005.04.004
PubMed: 15878637

Affiliations:

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Le document en format XML

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<series><title level="j">Biochimica et biophysica acta</title>
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<imprint><date when="2005" type="published">2005</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algorithms (MeSH)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Computational Biology (methods)</term>
<term>Computer Simulation (MeSH)</term>
<term>Conserved Sequence (MeSH)</term>
<term>Enzyme Activation (MeSH)</term>
<term>Glycoproteins (analysis)</term>
<term>Glycoproteins (chemistry)</term>
<term>Models, Chemical (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Plant Lectins (analysis)</term>
<term>Plant Lectins (chemistry)</term>
<term>Plant Proteins (analysis)</term>
<term>Plant Proteins (chemistry)</term>
<term>Populus (enzymology)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (analysis)</term>
<term>Protein-Serine-Threonine Kinases (chemistry)</term>
<term>Receptors, Cell Surface (analysis)</term>
<term>Receptors, Cell Surface (chemistry)</term>
<term>Sequence Alignment (methods)</term>
<term>Sequence Analysis, Protein (methods)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term>
<term>Algorithmes (MeSH)</term>
<term>Alignement de séquences (méthodes)</term>
<term>Analyse de séquence de protéine (méthodes)</term>
<term>Biologie informatique (méthodes)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glycoprotéines (analyse)</term>
<term>Glycoprotéines (composition chimique)</term>
<term>Lectines végétales (analyse)</term>
<term>Lectines végétales (composition chimique)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Modèles chimiques (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Populus (enzymologie)</term>
<term>Protein-Serine-Threonine Kinases (analyse)</term>
<term>Protein-Serine-Threonine Kinases (composition chimique)</term>
<term>Protéines végétales (analyse)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Récepteurs de surface cellulaire (analyse)</term>
<term>Récepteurs de surface cellulaire (composition chimique)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Simulation numérique (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
<term>Séquence conservée (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Glycoproteins</term>
<term>Plant Lectins</term>
<term>Plant Proteins</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Receptors, Cell Surface</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glycoproteins</term>
<term>Plant Lectins</term>
<term>Plant Proteins</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Receptors, Cell Surface</term>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Glycoprotéines</term>
<term>Lectines végétales</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines végétales</term>
<term>Récepteurs de surface cellulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glycoprotéines</term>
<term>Lectines végétales</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines végétales</term>
<term>Récepteurs de surface cellulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Computational Biology</term>
<term>Sequence Alignment</term>
<term>Sequence Analysis, Protein</term>
</keywords>
<keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Alignement de séquences</term>
<term>Analyse de séquence de protéine</term>
<term>Biologie informatique</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Algorithms</term>
<term>Amino Acid Sequence</term>
<term>Binding Sites</term>
<term>Computer Simulation</term>
<term>Conserved Sequence</term>
<term>Enzyme Activation</term>
<term>Models, Chemical</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term>
<term>Algorithmes</term>
<term>Données de séquences moléculaires</term>
<term>Liaison aux protéines</term>
<term>Modèles chimiques</term>
<term>Modèles moléculaires</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Simulation numérique</term>
<term>Sites de fixation</term>
<term>Séquence conservée</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Detection of genes for putative receptor-like protein kinases, which contain an extracellular domain related to leguminous lectins, in plant genomes inspired the hypothesis that this part acts as sensor. Initial support for this concept came from proof for protein kinase activity. The next step, focusing on the protein of lombardy poplar (Populus nigra var. italica), is scrutiny for lectin activity. Consequently, we first pinpointed sets of high-scoring sequence pairs by extensive databank search. The calculations resulted in P-values in the range from 10(-14) to 10(-18) exclusively for leguminous lectins, the Pterocarpus angolensis agglutinin being front runner with P=3 x 10(-18) and thus most suitable template for modeling. The superimposition of the two folds gave notable similarity in the region responsible for binding carbohydrate and Ca(2+)/Mn(2+)-ions. Binding activity toward carbohydrates was detected by assaying a panel of (neo)glycoproteins as polyvalent probes, especially for alpha-l-rhamnose and glycans of asialofetuin. It was strictly dependent on Ca(2+)-ions, enhanced by Mn(2+)-ions and reached a K(D)-value of 34.3 nM for the neoglycoprotein with rhamnose as ligand. These results give further research direction to define physiological ligands, plant/bacterial rhamnose-containing saccharides and rhamnose-mimetic glycans or peptides being potential candidates.</div>
</front>
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<Abstract><AbstractText>Detection of genes for putative receptor-like protein kinases, which contain an extracellular domain related to leguminous lectins, in plant genomes inspired the hypothesis that this part acts as sensor. Initial support for this concept came from proof for protein kinase activity. The next step, focusing on the protein of lombardy poplar (Populus nigra var. italica), is scrutiny for lectin activity. Consequently, we first pinpointed sets of high-scoring sequence pairs by extensive databank search. The calculations resulted in P-values in the range from 10(-14) to 10(-18) exclusively for leguminous lectins, the Pterocarpus angolensis agglutinin being front runner with P=3 x 10(-18) and thus most suitable template for modeling. The superimposition of the two folds gave notable similarity in the region responsible for binding carbohydrate and Ca(2+)/Mn(2+)-ions. Binding activity toward carbohydrates was detected by assaying a panel of (neo)glycoproteins as polyvalent probes, especially for alpha-l-rhamnose and glycans of asialofetuin. It was strictly dependent on Ca(2+)-ions, enhanced by Mn(2+)-ions and reached a K(D)-value of 34.3 nM for the neoglycoprotein with rhamnose as ligand. These results give further research direction to define physiological ligands, plant/bacterial rhamnose-containing saccharides and rhamnose-mimetic glycans or peptides being potential candidates.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>André</LastName>
<ForeName>Sabine</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 München, Germany. Sabine.Andre@lmu.de</Affiliation>
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<Author ValidYN="Y"><LastName>Tazaki</LastName>
<ForeName>Kiyoshi</ForeName>
<Initials>K</Initials>
</Author>
<Author ValidYN="Y"><LastName>Gabius</LastName>
<ForeName>Hans-Joachim</ForeName>
<Initials>HJ</Initials>
</Author>
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<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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</Chemical>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
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</MeshHeading>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
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<MeshHeading><DescriptorName UI="D011956" MajorTopicYN="N">Receptors, Cell Surface</DescriptorName>
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<QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName>
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<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName>
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<tree><noCountry><name sortKey="Gabius, Hans Joachim" sort="Gabius, Hans Joachim" uniqKey="Gabius H" first="Hans-Joachim" last="Gabius">Hans-Joachim Gabius</name>
<name sortKey="Nishiguchi, Mitsuru" sort="Nishiguchi, Mitsuru" uniqKey="Nishiguchi M" first="Mitsuru" last="Nishiguchi">Mitsuru Nishiguchi</name>
<name sortKey="Siebert, Hans Christian" sort="Siebert, Hans Christian" uniqKey="Siebert H" first="Hans-Christian" last="Siebert">Hans-Christian Siebert</name>
<name sortKey="Tazaki, Kiyoshi" sort="Tazaki, Kiyoshi" uniqKey="Tazaki K" first="Kiyoshi" last="Tazaki">Kiyoshi Tazaki</name>
</noCountry>
<country name="Allemagne"><region name="Bavière"><name sortKey="Andre, Sabine" sort="Andre, Sabine" uniqKey="Andre S" first="Sabine" last="André">Sabine André</name>
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   |area=    PoplarV1
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   |type=    RBID
   |clé=     pubmed:15878637
   |texte=   Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.
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Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.

Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.

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