tailieunhanh - Báo cáo khoa học: A possible physiological function and the tertiary structure of a 4-kDa peptide in legumes

Previously, we isolated a 4-kDa peptide capable of binding to a 43-kDa receptor-like protein and stimulating protein kinase activity of the 43-kDa protein in soybean. Both of them were found to localize in the plasma membranes and cell walls. Here, we report the physiological effects of 4-kDa peptide expressed transiently in the cultured carrot and bird’s-foot trefoil cells transfected with pBI 121 plas-mid containing the 4-kDa peptide gene. | Eur. J. Biochem. 270 1269-1276 2003 FEBS 2003 doi A possible physiological function and the tertiary structure of a 4-kDa peptide in legumes Toshimasa Yamazaki1. Motoko Takaoka2 3 Etsuko Katoh1. Kazuki Hanada2. Masashi Sakita2 Kyoko Sakata2 Yuji Nishiuchi4 and Hisashi Hirano2 1 National Institute of Agrobiological Sciences Tsukuba Ibaraki Japan 2 Yokohama City University Kihara Institute for Biological Research Graduate School of Integrated Science Totsuka Yokohama Japan 3Kamakura Woman s University Iwase Kamakura Japan 4Peptide Institute Inc Protein Research Foundation Minoh Osaka Japan Previously we isolated a 4-kDa peptide capable of binding to a 43-kDa receptor-like protein and stimulating protein kinase activity of the 43-kDa protein in soybean. Both of them were found to localize in the plasma membranes and cell walls. Here we report the physiological effects of 4-kDa peptide expressed transiently in the cultured carrot and bird s-foot trefoil cells transfected with pBI 121 plasmid containing the 4-kDa peptide gene. At early developmental stage the transgenic callus grew rapidly compared to the wild callus in both species. Cell proliferation of in vitro cultured nonembryogenic carrot callus was apparently affected with the 4-kDa peptide in the medium. Complementary DNAs encoding the 4-kDa peptide from mung bean and azuki bean were cloned by PCR and sequenced. The amino-acid sequences deduced from the nucleotide sequences are homologous among legume species particularly the sites of cysteine residues are highly conserved. This conserved sequence reflects the importance of intradisulfide bonds required for the 4-kDa peptide to perform its function. Three dimensional structure of the 4-kDa peptide determined by NMR spectroscopy suggests that this peptide is a T-knot scaffold containing three b-strands and the specific binding activity to the 43-kDa protein and stimulatory effect on the protein phosphorylation could be attributed

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