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http://purl.uniprot.org/citations/1915286http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1915286http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1915286http://www.w3.org/2000/01/rdf-schema#comment"The rolB gene of Agrobacterium rhizogenes, whose expression stimulates the formation of roots by transformed plant tissues and other growth alterations in transgenic plants, codes for a beta-glucosidase able to hydrolyse indole-beta-glucosides. Indeed, we show that extracts of bacteria and/or plant tissue expressing the rolB protein hydrolyse indoxyl-beta-glucoside (plant indican). Because of the structural similarity between indoxyl-beta-glucoside and indole-3-acetyl-beta-glucoside (IAA-beta-glucoside), we propose that the physiological and developmental alterations in transgenic plants expressing the rolB gene could be the result of an increased intracellular auxin activity caused by the release of active auxins from inactive beta-glucosides. Thus two of the oncogenes carried by the T-DNA of the plant pathogen Agrobacterium rhizogenes (rolB and rolC) perturb plant growth and development by coding for beta-glucosidases with distinct specificities. Whereas the rolC beta-glucosidase releases cytokinins from their glucoside conjugates, the rolB encoded protein hydrolyses indole-beta-glucosides. The combined action of these two genes therefore is expected to modulate the intracellular concentration of two of the main growth factors active in plants."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1991.tb04873.x"xsd:string
http://purl.uniprot.org/citations/1915286http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1991.tb04873.x"xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/author"Schell J."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/author"Schell J."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/author"Estruch J.J."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/author"Estruch J.J."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/author"Spena A."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/author"Spena A."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/pages"3125-3128"xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/pages"3125-3128"xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/title"The protein encoded by the rolB plant oncogene hydrolyses indole glucosides."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/title"The protein encoded by the rolB plant oncogene hydrolyses indole glucosides."xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/1915286http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/1915286http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1915286
http://purl.uniprot.org/citations/1915286http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1915286
http://purl.uniprot.org/citations/1915286http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1915286
http://purl.uniprot.org/citations/1915286http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1915286