The S-locus receptor kinase gene in a self-incompatible Brassica napus line encodes a functional serine/threonine kinase.
Author(s) -
Daphne R. Goring,
Steven J. Rothstein
Publication year - 1992
Publication title -
the plant cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.324
H-Index - 341
eISSN - 1532-298X
pISSN - 1040-4651
DOI - 10.1105/tpc.4.10.1273
Subject(s) - biology , map2k7 , cyclin dependent kinase 9 , map kinase kinase kinase , threonine , c raf , akt3 , protein kinase domain , mitogen activated protein kinase kinase , microbiology and biotechnology , biochemistry , serine , kinase , gene , protein kinase a , cyclin dependent kinase 2 , phosphorylation , mutant
An S-receptor kinase (SRK) cDNA, SRK-910, from the active S-locus in a self-incompatible Brassica napus W1 line has been isolated and characterized. The SRK-910 gene is predominantly expressed in pistils and segregates with the W1 self-incompatibility phenotype in an F2 population derived from a cross between the self-incompatible W1 line and a self-compatible Westar line. Analysis of the predicted amino acid sequence demonstrated that the extracellular receptor domain is highly homologous to S-locus glycoproteins, whereas the cytoplasmic kinase domain contains conserved amino acids present in serine/threonine kinases. An SRK-910 kinase protein fusion was produced in Escherichia coli and found to contain kinase activity. Phosphoamino acid analysis confirmed that only serine and threonine residues were phosphorylated. Thus, the SRK-910 gene encodes a functional serine/threonine receptor kinase.
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