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The amino acid sequence of twenty residues from the N-termlnus of the regulatory subunit of cAMP-dependent protein kinase purified from the yeast Saccharomyces cerevisiae was reported several years ago (1). We prepared three corresponding ollgonucleotldes: one 23-base mixed sequence (128-fold degenerate) probe and two unique (45and 60-base) probes that accommodate the apparent codon usage bias of £. cerevisiae (2,3). The three synthetic probes were used to screen a yeast genomlc DNA library In the vector YCp50 (kindly provided by M. Rose). Two plasmlds were obtained that, by restriction endonuclease cleavage site mapping, contained a common segment of genomic DNA. Digests of this common region (Bglll, EcoRV, Ms£l, m i . Sau3A, ̂ p_hl, Xbal) were sub-cloned into M13mpl8 and M13mpl9 (4) and were sequenced on both strands by standard dideoxy chain termination methods (5). The open reading frame present encodes a 416-residue polypeptide that, aside from the Initiator methionlne, commences with a perfect match (underlined) to the N-termlnal sequence of the purified protein. Hybridization of the cloned gene to Southern blots of genomic DNA digests (6), to whole yeast chromosomes separated by orthogonal fieldalternation gel electrophoresls (7), and to polyA RNA species fractionated by by gel electrophoresis (8), demonstrated that the gene is a unique single-copy locus, resides on chromosome IX, and encodes a transcript of 1595 bases. Two mutations (bcyl and sral) known to affect the level of regulatory subunit (9,10) also map on chromosome IX and probably represent lesions In REG1. Computer comparison (ALIGN program of Intelligenetlcs, Inc.) indicates that the C-termlnal two-thirds of the yeast REG1 protein shares 40% Identity with both mammalian type I and type II regulatory subunlts (11,12). Homology is especially conserved around the residues known to be involved in cAMP binding (asterisks). Like the type II subunit, the predicted yeast protein has a potential phosphorylatlon site (P) in the domain corresponding to the "hinge region" thought to be the major site of Interaction with the catalytic subunit (13). The yeast REG1 protein can be phosphorylated In vitro by both the yeast (14) and bovine (1) catalytic subunit and appears to be phosphorylated In vivo (15).

nucleic acids research

Complete nucleotide sequence of the gene encoding the regulatory subunit of 3′,5′-cyclic AMP-dependent protein kinase from the yeast<i>Saccharomyces cerevisiae</i>

Complete nucleotide sequence of the gene encoding the regulatory subunit of 3′,5′-cyclic AMP-dependent protein kinase from the yeastSaccharomyces cerevisiae