Studies by site-directed mutagenesis of the carbohydrate-binding properties of a bark lectin from Robinia pseudoacacia.
Identifieur interne : 000464 ( Main/Exploration ); précédent : 000463; suivant : 000465Studies by site-directed mutagenesis of the carbohydrate-binding properties of a bark lectin from Robinia pseudoacacia.
Auteurs : M. Nishiguchi [Japon] ; K. Yoshida ; T. Sumizono ; K. TazakiSource :
- FEBS letters [ 0014-5793 ] ; 1997.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Arbres (composition chimique), Escherichia coli (MeSH), Lapins (MeSH), Lectines (composition chimique), Lectines (génétique), Lectines (isolement et purification), Lectines (métabolisme), Lectines végétales (MeSH), Liaison aux protéines (MeSH), Mannose (pharmacologie), Masse moléculaire (MeSH), Mutagenèse dirigée (MeSH), Métabolisme glucidique (MeSH), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (isolement et purification), Protéines de fusion recombinantes (métabolisme), Tests d'hémagglutination (MeSH), Érythrocytes (MeSH).
- MESH :
- composition chimique : Arbres, Lectines, Protéines de fusion recombinantes.
- génétique : Lectines.
- isolement et purification : Lectines, Protéines de fusion recombinantes.
- métabolisme : Lectines, Protéines de fusion recombinantes.
- pharmacologie : Mannose.
- Animaux, Escherichia coli, Lapins, Lectines végétales, Liaison aux protéines, Masse moléculaire, Mutagenèse dirigée, Métabolisme glucidique, Tests d'hémagglutination, Érythrocytes.
English descriptors
- KwdEn :
- Animals (MeSH), Carbohydrate Metabolism (MeSH), Erythrocytes (MeSH), Escherichia coli (MeSH), Hemagglutination Tests (MeSH), Lectins (chemistry), Lectins (genetics), Lectins (isolation & purification), Lectins (metabolism), Mannose (pharmacology), Molecular Weight (MeSH), Mutagenesis, Site-Directed (MeSH), Plant Lectins (MeSH), Protein Binding (MeSH), Rabbits (MeSH), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (isolation & purification), Recombinant Fusion Proteins (metabolism), Trees (chemistry).
- MESH :
- chemical , chemistry : Lectins, Recombinant Fusion Proteins.
- chemical , genetics : Lectins.
- chemical , isolation & purification : Lectins, Recombinant Fusion Proteins.
- chemical , metabolism : Lectins, Recombinant Fusion Proteins.
- chemical , pharmacology : Mannose.
- chemistry : Trees.
- Animals, Carbohydrate Metabolism, Erythrocytes, Escherichia coli, Hemagglutination Tests, Molecular Weight, Mutagenesis, Site-Directed, Plant Lectins, Protein Binding, Rabbits.
Abstract
A bark lectin, RBL, from Robinia pseudoacacia (black locust), binds galactose-related sugars specifically. Recombinant RBL (rRBL) with a histidine tag was expressed in Escherichia coli, purified and characterized. rRBL agglutinated rabbit erythrocytes and the hemagglutination was inhibited by galactose and related sugars. To elucidate the mechanism of the binding of carbohydrate by RBL, 16 mutant rRBLs were produced by site-directed mutagenesis. The analysis of the mutants indicated that residues Phe130 and Asp87 play key roles in the binding of carbohydrate by RBL. When Thu215, Leu217 and Ser218 in the carboxy-terminal region were replaced by alanine, the respective replacements decreased the hemagglutinating activity. However, replacement by alanine of Glu219 did not decrease this activity. Three mutant rRBLs were generated by reference to the primary sequences of the proposed carbohydrate- and metal-binding regions of mannose-specific lectins. Although these rRBLs agglutinated rabbit erythrocytes, the hemagglutination was not inhibited by mannose. Substitution or insertion that yielded a partial sequence similar to those of L-fucose-specific lectins and hemagglutinin from Maackia amurensis resulted in a complete loss of the hemagglutinating activity of rRBL.
DOI: 10.1016/s0014-5793(97)00068-9
PubMed: 9091320
Affiliations:
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Nishiguchi</name><affiliation wicri:level="1"><nlm:affiliation>Forestry and Forest Products Research Institute, Ibaraki, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Forestry and Forest Products Research Institute, Ibaraki</wicri:regionArea><wicri:noRegion>Ibaraki</wicri:noRegion></affiliation></author><author><name sortKey="Yoshida, K" sort="Yoshida, K" uniqKey="Yoshida K" first="K" last="Yoshida">K. Yoshida</name></author><author><name sortKey="Sumizono, T" sort="Sumizono, T" uniqKey="Sumizono T" first="T" last="Sumizono">T. Sumizono</name></author><author><name sortKey="Tazaki, K" sort="Tazaki, K" uniqKey="Tazaki K" first="K" last="Tazaki">K. Tazaki</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Carbohydrate Metabolism (MeSH)</term><term>Erythrocytes (MeSH)</term><term>Escherichia coli (MeSH)</term><term>Hemagglutination Tests (MeSH)</term><term>Lectins (chemistry)</term><term>Lectins (genetics)</term><term>Lectins (isolation & purification)</term><term>Lectins (metabolism)</term><term>Mannose (pharmacology)</term><term>Molecular Weight (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Plant Lectins (MeSH)</term><term>Protein Binding (MeSH)</term><term>Rabbits (MeSH)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (isolation & purification)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Trees (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Arbres (composition chimique)</term><term>Escherichia coli (MeSH)</term><term>Lapins (MeSH)</term><term>Lectines (composition chimique)</term><term>Lectines (génétique)</term><term>Lectines (isolement et purification)</term><term>Lectines (métabolisme)</term><term>Lectines végétales (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Mannose (pharmacologie)</term><term>Masse moléculaire (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Métabolisme glucidique (MeSH)</term><term>Protéines de fusion recombinantes (composition chimique)</term><term>Protéines de fusion recombinantes (isolement et purification)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Tests d'hémagglutination (MeSH)</term><term>Érythrocytes (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lectins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Lectins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Lectins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lectins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Mannose</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Trees</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Arbres</term><term>Lectines</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Lectines</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Lectines</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lectines</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Mannose</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Carbohydrate Metabolism</term><term>Erythrocytes</term><term>Escherichia coli</term><term>Hemagglutination Tests</term><term>Molecular Weight</term><term>Mutagenesis, Site-Directed</term><term>Plant Lectins</term><term>Protein Binding</term><term>Rabbits</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Escherichia coli</term><term>Lapins</term><term>Lectines végétales</term><term>Liaison aux protéines</term><term>Masse moléculaire</term><term>Mutagenèse dirigée</term><term>Métabolisme glucidique</term><term>Tests d'hémagglutination</term><term>Érythrocytes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A bark lectin, RBL, from Robinia pseudoacacia (black locust), binds galactose-related sugars specifically. Recombinant RBL (rRBL) with a histidine tag was expressed in Escherichia coli, purified and characterized. rRBL agglutinated rabbit erythrocytes and the hemagglutination was inhibited by galactose and related sugars. To elucidate the mechanism of the binding of carbohydrate by RBL, 16 mutant rRBLs were produced by site-directed mutagenesis. The analysis of the mutants indicated that residues Phe130 and Asp87 play key roles in the binding of carbohydrate by RBL. When Thu215, Leu217 and Ser218 in the carboxy-terminal region were replaced by alanine, the respective replacements decreased the hemagglutinating activity. However, replacement by alanine of Glu219 did not decrease this activity. Three mutant rRBLs were generated by reference to the primary sequences of the proposed carbohydrate- and metal-binding regions of mannose-specific lectins. Although these rRBLs agglutinated rabbit erythrocytes, the hemagglutination was not inhibited by mannose. Substitution or insertion that yielded a partial sequence similar to those of L-fucose-specific lectins and hemagglutinin from Maackia amurensis resulted in a complete loss of the hemagglutinating activity of rRBL.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9091320</PMID><DateCompleted><Year>1997</Year><Month>04</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>403</Volume><Issue>3</Issue><PubDate><Year>1997</Year><Month>Feb</Month><Day>24</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Studies by site-directed mutagenesis of the carbohydrate-binding properties of a bark lectin from Robinia pseudoacacia.</ArticleTitle><Pagination><MedlinePgn>294-8</MedlinePgn></Pagination><Abstract><AbstractText>A bark lectin, RBL, from Robinia pseudoacacia (black locust), binds galactose-related sugars specifically. Recombinant RBL (rRBL) with a histidine tag was expressed in Escherichia coli, purified and characterized. rRBL agglutinated rabbit erythrocytes and the hemagglutination was inhibited by galactose and related sugars. To elucidate the mechanism of the binding of carbohydrate by RBL, 16 mutant rRBLs were produced by site-directed mutagenesis. The analysis of the mutants indicated that residues Phe130 and Asp87 play key roles in the binding of carbohydrate by RBL. When Thu215, Leu217 and Ser218 in the carboxy-terminal region were replaced by alanine, the respective replacements decreased the hemagglutinating activity. However, replacement by alanine of Glu219 did not decrease this activity. Three mutant rRBLs were generated by reference to the primary sequences of the proposed carbohydrate- and metal-binding regions of mannose-specific lectins. Although these rRBLs agglutinated rabbit erythrocytes, the hemagglutination was not inhibited by mannose. Substitution or insertion that yielded a partial sequence similar to those of L-fucose-specific lectins and hemagglutinin from Maackia amurensis resulted in a complete loss of the hemagglutinating activity of rRBL.</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, Ibaraki, Japan.</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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037102">Lectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037121">Plant Lectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>PHA4727WTP</RegistryNumber><NameOfSubstance UI="D008358">Mannose</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050260" MajorTopicYN="Y">Carbohydrate Metabolism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006386" MajorTopicYN="N">Hemagglutination Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037102" MajorTopicYN="N">Lectins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008358" MajorTopicYN="N">Mannose</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037121" MajorTopicYN="N">Plant Lectins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011817" MajorTopicYN="N">Rabbits</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>2</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>2</Month><Day>24</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>2</Month><Day>24</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9091320</ArticleId><ArticleId IdType="pii">S0014-5793(97)00068-9</ArticleId><ArticleId IdType="doi">10.1016/s0014-5793(97)00068-9</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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