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http://purl.uniprot.org/citations/22193750http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22193750http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22193750http://www.w3.org/2000/01/rdf-schema#comment"β-conglycinin, a major seed protein in soybean, is composed of α, α', and β subunits sharing a high homology among them. Despite its many health benefits, β-conglycinin has a lower amino acid score and lower functional gelling properties compared to glycinin, another major soybean seed protein. In addition, the α, α', and β subunits also contain major allergens. A wild soybean (Glycine soja Sieb et Zucc.) line, 'QT2', lacks all of the β-conglycinin subunits, and the deficiency is controlled by a single dominant gene, Scg-1 (Suppressor of β-conglycinin). This gene was characterized using a soybean cultivar 'Fukuyutaka', 'QY7-25', (its near-isogenic line carrying the Scg-1 gene), and the F₂ population derived from them. The physical map of the Scg-1 region covered by lambda phage genomic clones revealed that the two α-subunit genes, a β-subunit gene, and a pseudo α-subunit gene were closely organized. The two α-subunit genes were arranged in a tail-to-tail orientation, and the genes were separated by 197 bp in Scg-1 compared to 3.3 kb in the normal allele (scg-1). In addition, small RNA was detected in immature seeds of the mutants by northern blot analysis using an RNA probe of the α subunit. These results strongly suggest that β-conglycinin deficiency in QT2 is controlled by post-transcriptional gene silencing through the inverted repeat of the α subunits."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.org/dc/terms/identifier"doi:10.1007/s11103-011-9865-y"xsd:string
http://purl.uniprot.org/citations/22193750http://purl.org/dc/terms/identifier"doi:10.1007/s11103-011-9865-y"xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Harada K."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Harada K."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Ishimoto M."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Ishimoto M."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Kanamori H."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Kanamori H."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Katayose Y."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Katayose Y."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Tsubokura Y."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Tsubokura Y."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Watanabe S."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Watanabe S."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Xia Z."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Xia Z."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Hajika M."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Hajika M."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Kaga A."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/author"Kaga A."xsd:string
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22193750http://purl.uniprot.org/core/date"2012"xsd:gYear