Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.
Identifieur interne : 004065 ( Main/Corpus ); précédent : 004064; suivant : 004066Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.
Auteurs : Sabine André ; Hans-Christian Siebert ; Mitsuru Nishiguchi ; Kiyoshi Tazaki ; Hans-Joachim GabiusSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2005.
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
Links to Exploration step
pubmed:15878637Le document en format XML
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Sabine.Andre@lmu.de</nlm:affiliation></affiliation></author><author><name sortKey="Siebert, Hans Christian" sort="Siebert, Hans Christian" uniqKey="Siebert H" first="Hans-Christian" last="Siebert">Hans-Christian Siebert</name></author><author><name sortKey="Nishiguchi, Mitsuru" sort="Nishiguchi, Mitsuru" uniqKey="Nishiguchi M" first="Mitsuru" last="Nishiguchi">Mitsuru Nishiguchi</name></author><author><name sortKey="Tazaki, Kiyoshi" sort="Tazaki, Kiyoshi" uniqKey="Tazaki K" first="Kiyoshi" last="Tazaki">Kiyoshi Tazaki</name></author><author><name sortKey="Gabius, Hans Joachim" sort="Gabius, Hans Joachim" uniqKey="Gabius H" first="Hans-Joachim" last="Gabius">Hans-Joachim Gabius</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15878637</idno><idno type="pmid">15878637</idno><idno type="doi">10.1016/j.bbagen.2005.04.004</idno><idno type="wicri:Area/Main/Corpus">004065</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004065</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.</title><author><name sortKey="Andre, Sabine" sort="Andre, Sabine" uniqKey="Andre S" first="Sabine" last="André">Sabine André</name><affiliation><nlm:affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 München, Germany. Sabine.Andre@lmu.de</nlm:affiliation></affiliation></author><author><name sortKey="Siebert, Hans Christian" sort="Siebert, Hans Christian" uniqKey="Siebert H" first="Hans-Christian" last="Siebert">Hans-Christian Siebert</name></author><author><name sortKey="Nishiguchi, Mitsuru" sort="Nishiguchi, Mitsuru" uniqKey="Nishiguchi M" first="Mitsuru" last="Nishiguchi">Mitsuru Nishiguchi</name></author><author><name sortKey="Tazaki, Kiyoshi" sort="Tazaki, Kiyoshi" uniqKey="Tazaki K" first="Kiyoshi" last="Tazaki">Kiyoshi Tazaki</name></author><author><name sortKey="Gabius, Hans Joachim" sort="Gabius, Hans Joachim" uniqKey="Gabius H" first="Hans-Joachim" last="Gabius">Hans-Joachim Gabius</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><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="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="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" 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></textClass></profileDesc></teiHeader><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></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15878637</PMID><DateCompleted><Year>2005</Year><Month>10</Month><Day>18</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1725</Volume><Issue>2</Issue><PubDate><Year>2005</Year><Month>Sep</Month><Day>15</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms.</ArticleTitle><Pagination><MedlinePgn>222-32</MedlinePgn></Pagination><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></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Siebert</LastName><ForeName>Hans-Christian</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Nishiguchi</LastName><ForeName>Mitsuru</ForeName><Initials>M</Initials></Author><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></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>2005</Year><Month>04</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006023">Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037121">Plant Lectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011956">Receptors, Cell Surface</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="D000465" MajorTopicYN="N">Algorithms</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid 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