The Saccharomyces cerevisiae SRK1 gene, a suppressor of bcy1 and ins1, may be involved in protein phosphatase function

The Saccharomyces cerevisiae SRK1 gene, when expressed on a low-copy shuttle vector, partially suppresses the phenotype associated with elevated levels of cyclic AMP-dependent protein kinase activity and suppresses the temperature-sensitive cell cycle arrest of the ins1 mutant. SRK1 is located on chromosome IV, 3 centimorgans from gcn2. A mutant carrying a deletion mutation in srk1 is viable. SRK1 encodes a 140-kDa protein with homology to the dis3+ protein from Schizosaccharomyces pombe. The ability of SRK1 to alleviate partially the defects caused by high levels of cyclic AMP-dependent protein kinase and the similarity of its encoded protein to dis3+ suggest that SRK1 may have a role in protein phosphatase function.

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Characterization of Saccharomyces cerevisiae genes encoding subunits of cyclic AMP-dependent protein kinase

Molecular and Cellular Biology ◽

10.1128/mcb.7.8.2653-2663.1987 ◽

1987 ◽

Vol 7 (8) ◽

pp. 2653-2663 ◽

Cited By ~ 1

Author(s):

J F Cannon ◽

K Tatchell

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Kinase ◽

Cyclic Amp ◽

Dna Sequences ◽

Regulatory Subunit ◽

Protein Kinase Activity ◽

Dependent Protein Kinase ◽

Ras Genes ◽

Camp Dependent Protein Kinase ◽

Dependent Protein

Mutations in the SRA1 or SRA3 gene eliminate the requirement for either RAS gene (RAS1 or RAS2) in Saccharomyces cerevisiae. We cloned SRA1 and SRA3 and determined their DNA sequences. SRA1 encodes the regulatory subunit of the cyclic AMP (cAMP)-dependent protein kinase and therefore is identical to REG1 and BCY1. This gene is not essential, but its deletion confers many traits: reduction of glycogen accumulation, temperature sensitivity, reduced growth rate on maltose and sucrose, inability to grow on galactose and nonfermentable carbon sources, and nitrogen starvation intolerance. SRA3 is homologous to protein kinases that phosphorylate serine and threonine and likely encodes the catalytic subunit of the cAMP-dependent protein kinase. The wild-type SRA3 gene either triplicated in the chromosome or on episomal, low-copy plasmids behaves like spontaneous dominant SRA3 mutations by suppressing ras2-530 (RAS2::LEU2 disruption), cdc25, and cdc35 mutations. These findings indicate that the yeast RAS genes are dispensable if there is constitutive cAMP-dependent protein kinase activity.

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Characterization of Saccharomyces cerevisiae genes encoding subunits of cyclic AMP-dependent protein kinase.

Molecular and Cellular Biology ◽

10.1128/mcb.7.8.2653 ◽

1987 ◽

Vol 7 (8) ◽

pp. 2653-2663 ◽

Cited By ~ 154

Author(s):

J F Cannon ◽

K Tatchell

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Kinase ◽

Cyclic Amp ◽

Dna Sequences ◽

Regulatory Subunit ◽

Protein Kinase Activity ◽

Dependent Protein Kinase ◽

Ras Genes ◽

Camp Dependent Protein Kinase ◽

Dependent Protein

Mutations in the SRA1 or SRA3 gene eliminate the requirement for either RAS gene (RAS1 or RAS2) in Saccharomyces cerevisiae. We cloned SRA1 and SRA3 and determined their DNA sequences. SRA1 encodes the regulatory subunit of the cyclic AMP (cAMP)-dependent protein kinase and therefore is identical to REG1 and BCY1. This gene is not essential, but its deletion confers many traits: reduction of glycogen accumulation, temperature sensitivity, reduced growth rate on maltose and sucrose, inability to grow on galactose and nonfermentable carbon sources, and nitrogen starvation intolerance. SRA3 is homologous to protein kinases that phosphorylate serine and threonine and likely encodes the catalytic subunit of the cAMP-dependent protein kinase. The wild-type SRA3 gene either triplicated in the chromosome or on episomal, low-copy plasmids behaves like spontaneous dominant SRA3 mutations by suppressing ras2-530 (RAS2::LEU2 disruption), cdc25, and cdc35 mutations. These findings indicate that the yeast RAS genes are dispensable if there is constitutive cAMP-dependent protein kinase activity.

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The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle.

Molecular and Cellular Biology ◽

10.1128/mcb.11.8.4045 ◽

1991 ◽

Vol 11 (8) ◽

pp. 4045-4052 ◽

Cited By ~ 86

Author(s):

S Garrett ◽

M M Menold ◽

J R Broach

Keyword(s):

Cell Cycle ◽

Protein Kinase ◽

Kinase Activity ◽

Specific Activity ◽

S Phase ◽

Protein Kinase Activity ◽

Dependent Protein Kinase ◽

Protein Levels ◽

Cycle Arrest ◽

Dependent Protein

Null mutations in the gene YAK1, which encodes a protein with sequence homology to known protein kinases, suppress the cell cycle arrest phenotype of mutants lacking the cyclic AMP-dependent protein kinase (A kinase). That is, loss of the YAK1 protein specifically compensates for loss of the A kinase. Here, we show that the protein encoded by YAK1 has protein kinase activity. Yak1 kinase activity is low during exponential growth but is induced at least 50-fold by arrest of cells prior to the completion of S phase. Induction is not observed by arrest at stages later in the cell cycle. Depending on the arrest regimen, induction can occur either by an increase in Yak1 protein levels or by an increase in Yak1 specific activity. Finally, an increase in Yak1 protein levels causes growth arrest of cells with attenuated A kinase activity. These results suggest that Yak1 acts in a pathway parallel to that of the A kinase to negatively regulate cell proliferation.

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The role of protein kinase activation in the control of steroidogenesis by adrenocorticotrophic hormone in the adrenal cortex

Biochemical Journal ◽

10.1042/bj1360993 ◽

1973 ◽

Vol 136 (4) ◽

pp. 993-998 ◽

Cited By ~ 29

Author(s):

Malcolm C. Richardson ◽

Dennis Schulster

Keyword(s):

Protein Kinase ◽

Cyclic Amp ◽

Adrenal Cortex ◽

Kinase Activity ◽

Protein Kinase Activity ◽

Adrenocorticotrophic Hormone ◽

Dependent Protein Kinase ◽

Kinase Activation ◽

Protein Kinase Activation ◽

Dependent Protein

A method has been developed for investigation of the effect of adrenocorticotrophic hormone (ACTH) on the state of activation of a cyclic AMP-dependent protein kinase within cells of the adrenal cortex. Enzyme activity was measured in terms of the quantity of32P transferred from [γ-32P]ATP to histone under conditions in which bound cyclic AMP did not dissociate from the regulatory subunit of the protein kinase ACTH (1×10-2i.u./ml) caused a rapid and complete activation of the cyclic AMP-dependent protein kinase activity within 2min of hormone addition to the isolated cells. In response to a range of ACTH concentrations a sigmoid log dose–response curve for protein kinase activation was obtained, with half-maximal stimulation attained at about 1×10-3i.u./ml. However, some low doses of ACTH that elicited a marked (but submaximal) steroidogenic response failed to cause a clear stimulation of protein kinase activity in isolated adrenal cells. Theophylline (2mm) potentiated the effect of ACTH on protein kinase activity. The results implicate an important role for protein kinase in ACTH action on the adrenocortical cell.

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Effect of thyroliberin on the concentration of adenosine 3′:5′-phosphate and on the activity of adenosine 3′:5′-phosphate-dependent protein kinase in prolactin-producing cells in culture

Biochemical Journal ◽

10.1042/bj1620379 ◽

1977 ◽

Vol 162 (2) ◽

pp. 379-386 ◽

Cited By ~ 30

Author(s):

K M Gautvik ◽

E Walaas ◽

O Walaas

Keyword(s):

Protein Kinase ◽

Cyclic Amp ◽

Time Course ◽

Pituitary Tumour ◽

Enzyme Activation ◽

Protein Kinase Activity ◽

Half Maximum ◽

Prolactin Release ◽

Dependent Protein Kinase ◽

Dependent Protein

1. The effects of thyroliberin were studied in cultured rat pituitary-tumour cells that synthesize and secrete prolactin (the GH4C1 cell strain). 2. Prolactin and cyclic AMP were measured by radioimmunological methods, and a cyclic AMP-dependent protein kinase was characterized by using histone as substrate. 3. Prolactin release was studied after 5-60min of treatment, and synthesis after 48h of treatment with thyroliberin. One-half maximum stimulation of release and synthesis were observed at 0.25 and at 4nM respectively. 4. Cyclic AMP was temporarily increased in cell suspensions after treatment with thyroliberin, and one-half maximum stimulation was observed at 25nM. 5. Dibutyryl cyclic AMP increased prolactin release and synthesis, one-half maximum effects being obtained at 20 micronM. 6. A cyclic AMP-dependent protein kinase, which was one-half maximally stimulated at 30 nM-cyclic AMP, was demonstrated. 7. An increase in the activity ratio (-cyclic AMP/+cyclic AMP) of the cyclic AMP-dependent protein kinase was observed after treatment with thyroliberin. Total protein kinase activity in the presence of cyclic AMP was unaltered. The time-course of enzyme activation was similar to that of cyclic AMP formation and corresponded to the time when prolactin release was first observed. 8. It is concluded that thyroliberin induces cyclic AMP formation, resulting in the activation of a cyclic AMP-dependent protein kinase.

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Cloning and characterization of BCY1, a locus encoding a regulatory subunit of the cyclic AMP-dependent protein kinase in Saccharomyces cerevisiae.

Molecular and Cellular Biology ◽

10.1128/mcb.7.4.1371 ◽

1987 ◽

Vol 7 (4) ◽

pp. 1371-1377 ◽

Cited By ~ 313

Author(s):

T Toda ◽

S Cameron ◽

P Sass ◽

M Zoller ◽

J D Scott ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Kinase ◽

Cyclic Amp ◽

Carbon Sources ◽

Regulatory Subunit ◽

Dependent Protein Kinase ◽

Yeast Saccharomyces Cerevisiae ◽

Regulatory Subunits ◽

Dependent Protein

We have cloned a gene (BCY1) from the yeast Saccharomyces cerevisiae that encodes a regulatory subunit of the cyclic AMP-dependent protein kinase. The encoded protein has a structural organization similar to that of the RI and RII regulatory subunits of the mammalian cyclic AMP-dependent protein kinase. Strains of S. cerevisiae with disrupted BCY1 genes do not display a cyclic AMP-dependent protein kinase in vitro, fail to grow on many carbon sources, and are exquisitely sensitive to heat shock and starvation.

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