Novel Family of Lectins Evolutionarily Related to Class V Chitinases: An Example of Neofunctionalization in Legumes
A lectin has been identified in black locust (Robinia pseudoacacia) bark that shares approximately 50% sequence identity with plant class V chitinases but is essentially devoid of chitinase activity. Specificity studies indicated that the black locust chitinase-related agglutinin (RobpsCRA) preferen...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2007-06, Vol.144 (2), p.662-672 |
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| container_title | Plant physiology (Bethesda) |
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| creator | Van Damme, Els J.M Culerrier, Raphaël Barre, Annick Alvarez, Richard Rougé, Pierre Peumans, Willy J |
| description | A lectin has been identified in black locust (Robinia pseudoacacia) bark that shares approximately 50% sequence identity with plant class V chitinases but is essentially devoid of chitinase activity. Specificity studies indicated that the black locust chitinase-related agglutinin (RobpsCRA) preferentially binds to high-mannose N-glycans comprising the proximal pentasaccharide core structure. Closely related orthologs of RobpsCRA could be identified in the legumes Glycine max, Medicago truncatula, and Lotus japonicus but in no other plant species, suggesting that this novel lectin family most probably evolved in an ancient legume species or possibly an earlier ancestor. This identification of RobpsCRA not only illustrates neofunctionalization in plants, but also provides firm evidence that plants are capable of developing a sugar-binding domain from an existing structural scaffold with a different activity and accordingly sheds new light on the molecular evolution of plant lectins. |
| doi_str_mv | 10.1104/pp.106.087981 |
| format | Article |
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Specificity studies indicated that the black locust chitinase-related agglutinin (RobpsCRA) preferentially binds to high-mannose N-glycans comprising the proximal pentasaccharide core structure. Closely related orthologs of RobpsCRA could be identified in the legumes Glycine max, Medicago truncatula, and Lotus japonicus but in no other plant species, suggesting that this novel lectin family most probably evolved in an ancient legume species or possibly an earlier ancestor. This identification of RobpsCRA not only illustrates neofunctionalization in plants, but also provides firm evidence that plants are capable of developing a sugar-binding domain from an existing structural scaffold with a different activity and accordingly sheds new light on the molecular evolution of plant lectins.</description><identifier>ISSN: 0032-0889</identifier><identifier>ISSN: 1532-2548</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.106.087981</identifier><identifier>PMID: 17098856</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Biologists</publisher><subject>Agglutinins ; Amino Acid Sequence ; Amino acids ; Bark ; Biological and medical sciences ; Biological Evolution ; Carbohydrate Metabolism ; Chitin ; Chitinases - chemistry ; Chitinases - metabolism ; Cloning, Molecular ; Evolution ; Focus Issue on Legume Biology ; Fundamental and applied biological sciences. Psychology ; Glycine max ; Lectins ; Legumes ; Lotus japonicus ; Medicago truncatula ; Models, Molecular ; Molecular Sequence Data ; Multigene Family ; Nicotiana - chemistry ; Nicotiana - enzymology ; Parasitism and symbiosis ; Plant Bark - chemistry ; Plant Bark - metabolism ; Plant Lectins - chemistry ; Plant Lectins - genetics ; Plant Lectins - metabolism ; Plant physiology and development ; Plants ; Polysaccharides ; Proteins ; Robinia - chemistry ; Robinia - genetics ; Robinia - metabolism ; Robinia pseudoacacia ; Sequence Homology, Amino Acid ; Symbiosis</subject><ispartof>Plant physiology (Bethesda), 2007-06, Vol.144 (2), p.662-672</ispartof><rights>Copyright 2007 American Society of Plant Biologists</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c539t-94710d3999ed7554b91306232c8c2ad7ab2805f6cf159dfef6ba41786e0c49d33</citedby><cites>FETCH-LOGICAL-c539t-94710d3999ed7554b91306232c8c2ad7ab2805f6cf159dfef6ba41786e0c49d33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/40065519$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/40065519$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>315,782,786,805,27931,27932,58024,58257</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18846698$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17098856$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van Damme, Els J.M</creatorcontrib><creatorcontrib>Culerrier, Raphaël</creatorcontrib><creatorcontrib>Barre, Annick</creatorcontrib><creatorcontrib>Alvarez, Richard</creatorcontrib><creatorcontrib>Rougé, Pierre</creatorcontrib><creatorcontrib>Peumans, Willy J</creatorcontrib><title>Novel Family of Lectins Evolutionarily Related to Class V Chitinases: An Example of Neofunctionalization in Legumes</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>A lectin has been identified in black locust (Robinia pseudoacacia) bark that shares approximately 50% sequence identity with plant class V chitinases but is essentially devoid of chitinase activity. Specificity studies indicated that the black locust chitinase-related agglutinin (RobpsCRA) preferentially binds to high-mannose N-glycans comprising the proximal pentasaccharide core structure. Closely related orthologs of RobpsCRA could be identified in the legumes Glycine max, Medicago truncatula, and Lotus japonicus but in no other plant species, suggesting that this novel lectin family most probably evolved in an ancient legume species or possibly an earlier ancestor. This identification of RobpsCRA not only illustrates neofunctionalization in plants, but also provides firm evidence that plants are capable of developing a sugar-binding domain from an existing structural scaffold with a different activity and accordingly sheds new light on the molecular evolution of plant lectins.</description><subject>Agglutinins</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Bark</subject><subject>Biological and medical sciences</subject><subject>Biological Evolution</subject><subject>Carbohydrate Metabolism</subject><subject>Chitin</subject><subject>Chitinases - chemistry</subject><subject>Chitinases - metabolism</subject><subject>Cloning, Molecular</subject><subject>Evolution</subject><subject>Focus Issue on Legume Biology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycine max</subject><subject>Lectins</subject><subject>Legumes</subject><subject>Lotus japonicus</subject><subject>Medicago truncatula</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>Nicotiana - chemistry</subject><subject>Nicotiana - enzymology</subject><subject>Parasitism and symbiosis</subject><subject>Plant Bark - chemistry</subject><subject>Plant Bark - metabolism</subject><subject>Plant Lectins - chemistry</subject><subject>Plant Lectins - genetics</subject><subject>Plant Lectins - metabolism</subject><subject>Plant physiology and development</subject><subject>Plants</subject><subject>Polysaccharides</subject><subject>Proteins</subject><subject>Robinia - chemistry</subject><subject>Robinia - genetics</subject><subject>Robinia - metabolism</subject><subject>Robinia pseudoacacia</subject><subject>Sequence Homology, Amino Acid</subject><subject>Symbiosis</subject><issn>0032-0889</issn><issn>1532-2548</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EosvCkSPgC9yyjONvbtVqC0irIgHlGnkdu6Ry4tROKspfj5es6JHTPOn95o00D6GXBDaEAHs_jhsCYgNKakUeoRXhtK5qztRjtAIoGpTSZ-hZzjcAQChhT9EZkaCV4mKF8mW8cwFfmL4L9zh6vHd26oaMd3cxzFMXB5OOzlcXzORaPEW8DSZn_ANvf3aFNNnlD_h8wLtfph-DO2Zcuujnwf7dDt1vcxS4G0r29dy7_Bw98SZk9-I01-jqYvd9-6naf_n4eXu-ryyneqo0kwRaqrV2reScHTShIGpaW2Vr00pzqBVwL6wnXLfeeXEwjEglHFimW0rX6N2SO6Z4O7s8NX2XrQvBDC7OuZEgSHkR-y9YA9OKclHAagFtijkn55sxdb1J9w2B5lhHM45Fimapo_CvT8HzoXftA336fwHengCTrQk-mcF2-YFTiglRbq_Rq4W7yVNM_3wGIDgnuvhvFt-b2JjrVDKuvtWlbgCpiNSc_gFg3aVk</recordid><startdate>20070601</startdate><enddate>20070601</enddate><creator>Van Damme, Els J.M</creator><creator>Culerrier, Raphaël</creator><creator>Barre, Annick</creator><creator>Alvarez, Richard</creator><creator>Rougé, Pierre</creator><creator>Peumans, Willy J</creator><general>American Society of Plant Biologists</general><general>American Society of Plant Physiologists</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20070601</creationdate><title>Novel Family of Lectins Evolutionarily Related to Class V Chitinases: An Example of Neofunctionalization in Legumes</title><author>Van Damme, Els J.M ; Culerrier, Raphaël ; Barre, Annick ; Alvarez, Richard ; Rougé, Pierre ; Peumans, Willy J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c539t-94710d3999ed7554b91306232c8c2ad7ab2805f6cf159dfef6ba41786e0c49d33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Agglutinins</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Bark</topic><topic>Biological and medical sciences</topic><topic>Biological Evolution</topic><topic>Carbohydrate Metabolism</topic><topic>Chitin</topic><topic>Chitinases - chemistry</topic><topic>Chitinases - metabolism</topic><topic>Cloning, Molecular</topic><topic>Evolution</topic><topic>Focus Issue on Legume Biology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycine max</topic><topic>Lectins</topic><topic>Legumes</topic><topic>Lotus japonicus</topic><topic>Medicago truncatula</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>Nicotiana - chemistry</topic><topic>Nicotiana - enzymology</topic><topic>Parasitism and symbiosis</topic><topic>Plant Bark - chemistry</topic><topic>Plant Bark - metabolism</topic><topic>Plant Lectins - chemistry</topic><topic>Plant Lectins - genetics</topic><topic>Plant Lectins - metabolism</topic><topic>Plant physiology and development</topic><topic>Plants</topic><topic>Polysaccharides</topic><topic>Proteins</topic><topic>Robinia - chemistry</topic><topic>Robinia - genetics</topic><topic>Robinia - metabolism</topic><topic>Robinia pseudoacacia</topic><topic>Sequence Homology, Amino Acid</topic><topic>Symbiosis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Damme, Els J.M</creatorcontrib><creatorcontrib>Culerrier, Raphaël</creatorcontrib><creatorcontrib>Barre, Annick</creatorcontrib><creatorcontrib>Alvarez, Richard</creatorcontrib><creatorcontrib>Rougé, Pierre</creatorcontrib><creatorcontrib>Peumans, Willy J</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van Damme, Els J.M</au><au>Culerrier, Raphaël</au><au>Barre, Annick</au><au>Alvarez, Richard</au><au>Rougé, Pierre</au><au>Peumans, Willy J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel Family of Lectins Evolutionarily Related to Class V Chitinases: An Example of Neofunctionalization in Legumes</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2007-06-01</date><risdate>2007</risdate><volume>144</volume><issue>2</issue><spage>662</spage><epage>672</epage><pages>662-672</pages><issn>0032-0889</issn><issn>1532-2548</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>A lectin has been identified in black locust (Robinia pseudoacacia) bark that shares approximately 50% sequence identity with plant class V chitinases but is essentially devoid of chitinase activity. Specificity studies indicated that the black locust chitinase-related agglutinin (RobpsCRA) preferentially binds to high-mannose N-glycans comprising the proximal pentasaccharide core structure. Closely related orthologs of RobpsCRA could be identified in the legumes Glycine max, Medicago truncatula, and Lotus japonicus but in no other plant species, suggesting that this novel lectin family most probably evolved in an ancient legume species or possibly an earlier ancestor. This identification of RobpsCRA not only illustrates neofunctionalization in plants, but also provides firm evidence that plants are capable of developing a sugar-binding domain from an existing structural scaffold with a different activity and accordingly sheds new light on the molecular evolution of plant lectins.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Biologists</pub><pmid>17098856</pmid><doi>10.1104/pp.106.087981</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Plant physiology (Bethesda), 2007-06, Vol.144 (2), p.662-672 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; JSTOR Archive Collection A-Z Listing; Oxford University Press Journals All Titles (1996-Current) |
| subjects | Agglutinins Amino Acid Sequence Amino acids Bark Biological and medical sciences Biological Evolution Carbohydrate Metabolism Chitin Chitinases - chemistry Chitinases - metabolism Cloning, Molecular Evolution Focus Issue on Legume Biology Fundamental and applied biological sciences. Psychology Glycine max Lectins Legumes Lotus japonicus Medicago truncatula Models, Molecular Molecular Sequence Data Multigene Family Nicotiana - chemistry Nicotiana - enzymology Parasitism and symbiosis Plant Bark - chemistry Plant Bark - metabolism Plant Lectins - chemistry Plant Lectins - genetics Plant Lectins - metabolism Plant physiology and development Plants Polysaccharides Proteins Robinia - chemistry Robinia - genetics Robinia - metabolism Robinia pseudoacacia Sequence Homology, Amino Acid Symbiosis |
| title | Novel Family of Lectins Evolutionarily Related to Class V Chitinases: An Example of Neofunctionalization in Legumes |
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