Amino acid residues on the surface of soybean 4-kDa peptide involved in the interaction with its binding protein

European Journal of Biochemistry

Volumn 270, Issue 12, 2003, Pages 2583-2592

  Hanada, Kazuki ^a   Nishiuchi, Yuji ^b   Hirano, Hisashi ^a  

^a YOKOHAMA CITY UNIVERSITY   (Japan)

^b Protein Research Foundation   (Japan)

Author keywords

Alanine scanning mutagenesis; Hormone like peptide; Protein protein interaction; Receptor like protein; Surface plasmon resonance

Indexed keywords

ALANINE; AMINO ACID; BINDING PROTEIN; DIMER; PEPTIDE; PROTEIN;

AMINO ACID ANALYSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CYTOPLASM; DISULFIDE BOND; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; HYDROPHOBICITY; IMMUNOASSAY; MASS SPECTROMETRY; MOLECULAR WEIGHT; MUTAGENESIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; PROTEIN VARIANT; SOYBEAN; SURFACE PLASMON RESONANCE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; CARRIER PROTEINS; DNA PRIMERS; MODELS, MOLECULAR; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PLANT PROTEINS; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; PROTEIN KINASES; RECOMBINANT PROTEINS; SOYBEANS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SURFACE PLASMON RESONANCE; VARIATION (GENETICS);

ESCHERICHIA COLI; GLYCINE MAX;

EID: 0037974456     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03627.x     Document Type: Article

References (22)

1. Komatsu, S., Koshio, O. & Hirano, H. (1994) Protein kinase activity and insulin-binding activity in plant basic 7S globulin. Biosci. Biotechnol. Biochem. 58, 1705-1706.
2. Satoh, S., Sturm, A., Fujii, T. & Chrispeels, M.J. (1992) cDNA cloning of an extracellular dermal glycoprotein of carrot and its expression in response to wounding. Planta 188, 432-438.
3. Kolivas, S. & Gayler, K.R. (1993) Structure of the cDNA coding for conglutin γ, a sulphur-rich protein from Lupinus angustifolius. Plant Mol. Biol. 21, 397-401.
4. Chung, R.P.-T., Neumann, G.M. & Polya, G.M. (1997) Purification and characterization of basic proteins with in vitro antifungal activity from seed of cotton, Gossypium hirsutum. Plant Sci. 127, 1-16.
5. Poltronieri, P., Cappello, M.S., Dohmae, N., Conti, A., Fortunato, D., Pastorello, E.A., Ortolani, C. & Zacheo, G. (2002) Identification and characterisation of the IgE-binding proteins 2S albumin and conglutin gamma in almond (Prunus dulcis) seeds. Int. Arch. Allergy Immunol. 128, 97-104.
6. Nishizawa, N.K., Mori, S., Watanabe, Y. & Hirano, H. (1994) Ultrastructural localization of the basic 7S globulin in soybean (Glycine max) cotyledons. Plant Cell Physiol. 35, 1079-1085.
7. Watanabe, Y., Barbashov, S.F., Komatsu, S., Hemmings, A.M., Miyagi, M., Tsunasawa, S. & Hirano, H. (1994) A peptide that stimulates phosphorylation of the plant insulin-binding protein: isolation, primary structure and cDNA cloning. Eur. J. Biochem. 224, 167-172.
8. Yamazaki, M., Takaoka, M., Katoh, E., Hanada, K., Sakita, M., Sakata, K., Nishiuchi, Y. & Hirano, H. (2003) A possible physiological function and the tertiary structure of a 4-kDa peptide in legumes. Eur. J. Biochem. 270, 1269-1276.
9. Lin, S.L. & Nussinov, R. (1995) A disulphide-reinforced structural scaffold shared by small proteins with diverse functions. Nat. Struct. Biol. 2, 835-837.
10. Higuchi, R., Krummel, B. & Saiki, R.K. (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucl. Acids Res. 16, 7351-7367.
11. Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. & Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
12. Alberts, B., Bray, D., Lewis, J., Raff, M., Roberts, K. & Watson, J.D. (2002) Molecular Biology of the Cell, 4th edn. Garland Publishing, New York.
13. Bessette, P.H., Åslund, F., Beckwith, J. & Georgiou, G. (1999) Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. USA 96, 13703-13708.
14. Stewart, E.J., Åslund, F. & Beckwith, J. (1998) Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J. 17, 5543-5550.
15. Mariuzza, R.A., Phillips, S.E. & Poljak, R.J. (1987) The structural basis of antigen-antibody recognition. Annu. Rev. Biophys. Biophys. Chem. 16, 139-159.
16. Wells, J.A. (1991) Systematic mutational analysis of protein-protein interfaces. Methods Enzymol. 202, 390-411.
17. Pittman, I., IV, Nakagawa, S.H., Tager, H.S. & Steiner, D.F. (1997) Maintenance of the B-chain beta-turn in [GlyB24] insulin mutants: a steady-state fluorescence anisotropy study. Biochemistry 36, 3430-3437.
18. Nakagawa, S.H. & Tager, H.S. (1986) Role of the phenylalanine B25 side chain in directing insulin interaction with its receptor: steric and conformational effects. J. Biol. Chem. 261, 7332-7341.
19. Nakagawa, S.H. & Tager, H.S. (1987) Role of the COOH-terminal B-chain domain in insulin-receptor interactions: identification of perturbations involving the insulin mainchain. J. Biol. Chem. 262, 12054-12058.
20. Mirmira, R.G., Nakagawa, S.H. & Tager, H.S. (1991) Importance of the character and configuration of residues B24, B25, and B26 in insulin-receptor interactions. J. Biol. Chem. 266, 1428-1436.
21. Mirmira, R.G. & Tager, H.S. (1989) Role of the phenylalanine B24 side chain in directing insulin interaction with its receptor: importance of main chain conformation. J. Biol. Chem. 264, 6349-6354.
22. Mirmira, R.G. & Tager, H.S. (1991) Disposition of the phenylalanine B25 side chain during insulin-receptor and insulin-insulin interactions. Biochemistry 30, 8222-8229.