Open AccessTwo yeast genes that encode unusual protein kinases.
Author(s) -
David E. Levin,
Charlotte I. Hammond,
Robert Ralston,
J M Bishop
Publication year - 1987
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.84.17.6035
Subject(s) - sh3 domain , biology , grb10 , cdc37 , gene , kinase , c raf , biochemistry , saccharomyces cerevisiae , homology (biology) , protein kinase a , receptor tyrosine kinase , genetics , mitogen activated protein kinase kinase , insulin resistance , extracellular signal regulated kinases , insulin , insulin receptor , endocrinology
Mixed synthetic oligonucleotides encoding sequences conserved among tyrosine-specific protein kinases were used to probe the genome of the budding yeast Saccharomyces cerevisiae. Two genes with homology to protein kinases were isolated and characterized by DNA sequence analysis. These genes, designated KIN1 and KIN2, are closely related to each other. Among previously characterized protein kinases, the products of KIN1 and KIN2 are most closely related to the bovine cAMP-dependent protein kinase (30% amino acid identities) and the protein encoded by the v-src oncogene (27% and 25% identities with KIN1 and KIN2, respectively) within their putative kinase domains. KIN1 and KIN2 are transcribed into 3.5-kilobase mRNAs that contain uninterrupted open reading frames encoding polypeptides of 117 kDa and 126 kDa, respectively. The predicted proteins are unusual in two respects: (i) their catalytic domains are carried near the N termini of relatively large proteins, in contrast to the majority of characterized protein kinases, and (ii) these catalytic domains are structural mosaics, with some features characteristic of tyrosine-specific protein kinases and other elements that are distinctive of serine/threonine-specific enzymes.