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Cloning and characterization of a wound‐specific hydroxyproline‐rich glycoprotein in Phaseolus vulgaris
Author(s) -
SAUER N.,
CORBIN D. R.,
KELLER B.,
LAMB C. J.
Publication year - 1990
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.1990.tb01310.x
Subject(s) - phaseolus , biology , amino acid , glycoprotein , hydroxyproline , proline , complementary dna , biochemistry , serine , microbiology and biotechnology , spore , ribonuclease , gene , botany , enzyme , rna
Abstract. We have isolated a cDNA clone whose corresponding transcript encodes an apoprotein of a hydroxyproline‐rich glycoprotein. Both infection of plants with fungal spores and treatment of suspension‐cultured bean cells with a fungal elicitor preparation cause a rapid decrease of the level of this mRNA. Wounding of bean tissue, however, leads to a very rapid, transient induction of this transcript. In contrast, all bean hydroxyproline‐rich glycoproteins described previously are induced both after infection with fungal spores and after mechanical damage. The protein encoded by this new clone contains a proline‐rich domain of about 30 kilodaltons. Most of these proline residues are part of the characteristic peptides Ser‐Pro 4 , Scr‐Pro 5 and Ser‐Pro 6 , which are often tandemly repeated. These tandem‐repeats are not found in any of the other bean hydroxyproline‐rich glycoproteins, where almost all of the Ser‐Pro 4 units are integrated into higher order repetitive units of 16 amino acids. The gene is present at a single or low copy number in the haploid genome and exhibits an unusual codon usage bias for the amino acids proline and serine.