Abstract
We have compared the partial nucleotide and derived amino acid sequences of a phaseolin seed storage protein gene ofPhaseolus vulgaris (1) and a conglycinin storage protein gene ofGlycine max (2). Although these proteins are not antigenically related to one another, the architecture of the genes is similar throughout the sequences compared here. Intervening sequences interrupt the same amino acid positions in both genes. Within the 28% of theG. max gene and the 38% of theP. vulgaris gene represented in this comparison, 73% of the nucleotides in the coding and intervening sequences are identical, excluding the insertions and deletions. The nucleotide mismatches found in the coding sequences are distributed throughout the three codon positions with little bias towards the third codon position. In addition to the single nucleotide differences, six insertions or deletions, ranging from three to twenty-seven nucleotides in length, occur in this portion of the coding region and these are partially responsible for the molecular weight differences of the conglycinin α′-subunit and the phaseolin subunit.
Similar content being viewed by others
References
Sun, SM, Slightom, JL & Hall, TC, 1981. Intervening sequences in a plant gene-comparison of the partial sequence of cDNA and genomic DNA of French bean phaseolin. Nature 289: 37–41.
Schuler, MA, Schmitt, ES & Beachy, RN, 1982. Closely related families of genes code for the α and α′ subunits of the soybean 7S storage protein complex. Nucleic Acids Res., in press.
Derbyshire, E, Wright, DJ & Boulter, D, 1976. Legumin and vicilin, storage proteins of legume seeds. Phytochem. 15: 3–24.
Dudman, WF & Millerd, A, 1975. Immunochemical behavior of legumin and vicilin from Vicia faba: a survey of related proteins in the leguminosae subfamily faboideae. Biochem. Syst. Eco. 3: 25–33.
Klozova, E & Kloz, J, 1972. Distribution of the protein ‘phaseolin’ in some representatives of Viciaceae. Biol. Plant. 14: 379–384.
Hill, JE & Breidenback, RW, 1974. Proteins of soybean seeds: 1. Isolation and characterization of the major components. Plant Physiol. 53: 742–746.
Gayler, KR & Sykes, GE, 1981. β-conglycinin in developing soybean seeds. Plant Physiol 67: 958–961.
Meinke, DW, Chen, J & Beachy, RN, 1981. Expression of storage protein genes during soybean seed development. Planta 153: 130–139.
Chrispeels, MJ, Higgins, TJV, Craig, S & Spencer, D, 1982. Role of the endoplasmic reticulum in the synthesis of reserve proteins and the kinetics of their transport to protein bodies in developing pea cotyledons. J. Cell Biol. 93: 5–14.
Chrispeels, MJ, Higgins, TJV & Spencer, D, 1982. Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J. Cell Biol. 93: 306–313.
Sun, SM, Mutschler, MA, Bliss, FA & Hall, TC, 1978. Protein synthesis and accumulation in bean cotyledons during growth. Plant Physiol. 61: 918–923.
McLeester, RC, Hall, TC, Sun, SM & Bliss, FA, 1973. Comparison of globulin proteins from Phaseolus vulgaris with those from Vicia faba. Phytochem. 12: 85–93.
Beachy, RN, Jarvis, NP & Barton, KA, 1981. Biosynthesis of subunits of the soybean 7S storage protein. J. Mol. Appl. Genet. 1: 19–27.
Brown, JMS, Bliss, FA & Hall, TC, 1981. Linkage relationships between genes controlling seed proteins in French bean. Theor. Appl. Genet. 60: 251–259.
Ma, Y, Bliss, FA & Hall, TC, 1980. Peptide mapping reveals considerable sequence homology among the three polypeptide subunits of G1 storage protein from French bean seed. Plant Physiol. 66: 897–902.
Bendich, AJ, Anderson, RS & Ward, BL, 1980. Plant DNA: long pure and simple. In: Leaver, CJ (ed.) Genome Organization and Expression in Plants. NATO, pp. 31–33.
Linguppa, VR, Linguppa, JR, Phased, R, Ebner, KE & Blobel, G, 1978. Coupled cell-free synthesis, segregation and core glycosylation of a secretory protein. Proc. Natl. Acad. Sci. USA 75: 2338–2342.
Voller, A, Bidwell, DE & Bartlett, A, 1979. The enzymelinked immunosorbent assay (ELISA). Dynatech Laboratories, Inc. Alexandria, Virginia.
Wahl, GM, Stern, M & Stark, GR, 1979. Efficient transfer of large DNA fragments from agarose gels to diazobenzylmethyl-paper and rapid hybridization using dextran sulfate. Proc. Natl. Acad. Sci. USA 76: 3683–3687.
Brown, WM, Prager, EM, Wang, A & Wilson, AC, 1982. Mitochondrial DNA sequences of primates: tempo and mode of evolution. J. Mol. Evol. 18: 225–239.
Perler, F, Efstratiadis, A, Lomedico, P, Gilbert, W, Kolodner, R & Dodgson, J, 1980. The evolution of genes: the chicken preproinsulin gene. Cell 20: 555–566.
Efstratiadis, A, Posakony, JW, Maniatis, T, Lawn, RM, O'Connell, C, Spritz, RA, DeRiel, JK, Forget, BG, Weissman, SM, Slightom, JL, Blechl, AE, Smithies, O, Bralle, FE, Shoulders, CC & Proudfoot, NJ, 1980. The structure and evolution of the human β-globin gene family. Cell 21: 653–668.
Shen, S, Slightom, JL & Smithies, O, 1981. A history of the human fetal globin gene duplication. Cell 26: 191–203.
Hall, L, Craig, RK, Edbrooke, MR & Campbell, PN, 1982. Comparison of the nucleotide sequence of cloned human and guinea-pig pre-α-lactalbumin cDNA with that of chick prelysozyme cDNA suggests evolution from a common ancestral gene. Nucleic Acids Res. 10: 3503–3515.
Sheppard, HW & Gutman, GA, 1981. Allelic forms of rat κ chain genes: evidence for strong selection at the level of nucleotide sequence. Proc. Natl. Acad. Sci. USA 78: 7064–7068.
Blackburn, DE, Hobbs, AA & Rosen, JM, 1982. Rat β-casein cDNA: sequence analysis and evolutionary comparisons. Nucleic Acids Res. 10: 2295–2307.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Schuler, M.A., Doyle, J.J. & Beachy, R.N. Nucleotide homologies between the glycosylated seed storage proteins ofGlycine max andPhaseolus vulgaris . Plant Mol Biol 2, 119–127 (1983). https://doi.org/10.1007/BF01578512
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF01578512