title: A peptide that stimulates phosphorylation of the plant insulin-binding protein. Isolation, primary structure and cDNA cloning.
abstract: The soybean seed basic 7S globulin (Bg) is capable of binding bovine insulin and insulin-like growth factors, and has protein kinase activity which corresponds to about two thirds of the tyrosine kinase activity of the rat insulin receptor. A 4-kDa peptide named leginsulin, which can bind to Bg and compete with insulin for binding to Bg, was isolated from radicles of germinated soybean seeds. The leginsulin had a stimulatory effect on the phosphorylation activity of Bg, suggesting that it is involved in cellular signal transduction. The leginsulin was sequenced by automated Edman degradation and electrospray ionization mass spectrometry. It consisted of 37 amino acid residues with six half-cystines in three disulfide bridges. The mass spectrometric analysis revealed that a portion of the peptide is processed to delete the C-terminal glycine like a number of animal peptide hormones, but not C-terminally amidated. The cDNA encoding the leginsulin was cloned, sequenced and considered to code for a precursor polypeptide consisting of a putative signal peptide, the leginsulin, a linker peptide, a 6-kDa peptide and a C-terminal peptide. Although there is no sequence similarity between the leginsulin and insulin or insulin-like growth factors, the leginsulin is a possible candidate for plant peptide hormones.
authors.affiliation: Department of Molecular Biology, National Institute of Agrobiological Resources, Tsukuba, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Watanabe
authors.forename: S F
authors.initials: SF
authors.lastname: Barbashov
authors.forename: S
authors.initials: S
authors.lastname: Komatsu
authors.forename: A M
authors.initials: AM
authors.lastname: Hemmings
authors.forename: M
authors.initials: M
authors.lastname: Miyagi
authors.forename: S
authors.initials: S
authors.lastname: Tsunasawa
authors.forename: H
authors.initials: H
authors.lastname: Hirano
mesh_terms: D000418:Albumins; D000595:Amino Acid Sequence; D000818:Animals; D052179:Antigens, Plant; D001483:Base Sequence; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002417:Cattle; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D005916:Globulins / Q000378:metabolism*; D007328:Insulin / Q000378:metabolism / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010766:Phosphorylation; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D055314:Seed Storage Proteins; D030262:Soybean Proteins; D013025:Glycine max
chemical_list: D000418:Albumins; D052179:Antigens, Plant; D002352:Carrier Proteins; D018076:DNA, Complementary; D005916:Globulins; D007328:Insulin; C089264:PA1 protein, Glycine max; D010940:Plant Proteins; D055314:Seed Storage Proteins; D030262:Soybean Proteins; C013894:beta-conglycinin protein, Glycine max