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http://purl.uniprot.org/citations/15564529http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15564529http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15564529http://www.w3.org/2000/01/rdf-schema#comment"Glycosyltransferases are enzymes that catalyze the attachment of a sugar molecule to specific acceptor molecules. These enzymes have been shown to play important roles in a number of biological processes. Whereas a large number of putative glycosyltransferase genes have been identified by genomic sequencing, the functions of most of these genes are unknown. Here we report the characterization of an Arabidopsis mutant, designated gaolaozhuangren1 (glz1), which is allelic to parvus characterized recently. The glz1 mutant exhibited a reduced plant stature, reduced size of organs in the shoot and dark-green leaves, indicating an important role of GLZ1 gene in normal development. The earliest GLZ1 expression appears at the shoot apical region of 4-d-old seedlings, which coincides with the onset of the glz1 morphological phenotypes. GLZ1 is expressed in a tissue-specific and developmentally regulated manner, predominantly in the stem and silique, and moderately in the flower. GLZ1 expression is strong in the midrib of rosette and cauline leaves; however, its expression was not detectable in the midrib of the cotyledon. Further analyses revealed that carbohydrate composition and distribution were aberrant in the glz1 mutant. These, together with the GLZ1 expression pattern, suggest a requirement for the GLZ1 function in normal sink-source transition during plant development."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pch168"xsd:string
http://purl.uniprot.org/citations/15564529http://purl.org/dc/terms/identifier"doi:10.1093/pcp/pch168"xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Hu Y."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Hu Y."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Huang H."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Huang H."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Liu D."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Liu D."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Ma H."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Ma H."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Zheng H."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Zheng H."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Jang J.C."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Jang J.C."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Shao M."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/author"Shao M."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/name"Plant Cell Physiol."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/name"Plant Cell Physiol."xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/pages"1453-1460"xsd:string
http://purl.uniprot.org/citations/15564529http://purl.uniprot.org/core/pages"1453-1460"xsd:string