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Molecular Characterization of Oat Seed Globulins
Author(s) -
Mark A. Shotwell,
Claudio Afonso,
Eric Davies,
Ruth S. Chesnut,
Brian A. Larkins
Publication year - 1988
Publication title -
plant physiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.87.3.698
Subject(s) - storage protein , glutelin , complementary dna , biology , amino acid , globulin , legumin , peptide sequence , gene , cdna library , signal peptide , microbiology and biotechnology , biochemistry , genome , nucleic acid sequence , genetics , immunology
We have isolated full-length cDNA clones that encode oat (Avena sativa) seed storage globulin mRNAs from a cDNA library in the expression vector lambda gtll. The longest of these clones, pOG2, has an 1840-base pair insert that encodes a complete precursor subunit with a signal peptide of 24 amino acids followed by an acidic polypeptide of 293 amino acids and a basic polypeptide of 201 amino acids. Near the C terminus of the acidic polypeptide are four repeats of a highly conserved, glutamine-rich octapeptide. Other oat globulin cDNA clones contain five of these repeats. Nucleotide sequence comparisons between these clones indicate that the genes encoding these proteins are highly conserved. We estimate there to be 7 to 10 genes for the oat globulin per haploid genome. Comparisons of amino acid sequences show that the oat globulin is 30 to 40% homologous with storage globulins of legumes and about 70% homologous with the rice seed storage globulin (glutelin).

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