|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
12
|
|
pubmed:dateCreated |
1991-12-19
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
In fission yeast, meiosis is initiated by transcriptional activation of the mei3+ gene under the combined influence of the four mating type genes. The mei3+ gene product acts as a meiotic inducer by binding to and inhibiting the ran1+ protein kinase. Inactivation of ran1+ kinase is both necessary and sufficient to allow meiotic differentiation. We describe a class of mutants which are unable to undergo both normal meiosis and meiosis induced by inactivation of ran1+. In addition to these defects, the cells are sterile and unable to enter stationary phase. We have determined that the mutants define two complementation groups, designated cgs1+ and cgs2+ (continues to grow in stationary). The wild type allele of each gene has been isolated and sequence analysis of cgs1+ shows that it encodes a protein homologous to the regulatory subunit of cyclic AMP dependent protein kinase (cAPK). Biochemical studies demonstrate that in cgs1-1 containing cells, cAPK activity is unregulated by cyclic AMP (cAMP). Sequence analysis of cgs2+ shows that the predicted protein it encodes shares homology with a phosphodiesterase from Dictyostelium discoideum and biochemical studies demonstrate that cells containing a mutant allele of cgs2+ have elevated levels of cAMP. Thus, both genes encode proteins that regulate the activity of cAPK. We have previously shown that cells overproducing ran1+ kinase are meiotically defective. Here, we provide direct evidence that the meiotic defect caused by either unregulated cAPK activity or unregulated ran1+ kinase activity is due to inability to induce transcription of the mei2+ gene, which is required for meiotic initiation. We propose that the switch from vegetative growth to meiosis in fission yeast requires inactivation of ran1+ kinase and is prevented by unregulated levels of cAPK.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-16593556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-2184942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-2328719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-2673232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-2840284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-2900761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-2972578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3010354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3025190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3034608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3037314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3200828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3288629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3323819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3357510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3511044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3830131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-3870979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-5743433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-6294466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-6310324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-6386045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-6526270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1657594-872891
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0261-4189
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
10
|
|
pubmed:geneSymbol |
cgs1<up>+</up>,
cgs2<up>+</up>,
ran1<up>+</up>
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
3759-68
|
|
pubmed:dateRevised |
2010-9-7
|
|
pubmed:meshHeading |
pubmed-meshheading:1657594-Amino Acid Sequence,
pubmed-meshheading:1657594-Base Sequence,
pubmed-meshheading:1657594-Blotting, Northern,
pubmed-meshheading:1657594-Cloning, Molecular,
pubmed-meshheading:1657594-Cyclic AMP,
pubmed-meshheading:1657594-DNA,
pubmed-meshheading:1657594-Genes, Fungal,
pubmed-meshheading:1657594-Genes, Mating Type, Fungal,
pubmed-meshheading:1657594-Meiosis,
pubmed-meshheading:1657594-Microscopy, Fluorescence,
pubmed-meshheading:1657594-Molecular Sequence Data,
pubmed-meshheading:1657594-Mutation,
pubmed-meshheading:1657594-Plasmids,
pubmed-meshheading:1657594-Protein Kinases,
pubmed-meshheading:1657594-RNA, Fungal,
pubmed-meshheading:1657594-Schizosaccharomyces,
pubmed-meshheading:1657594-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1657594-Spores, Fungal
|
|
pubmed:year |
1991
|
|
pubmed:articleTitle |
Interaction between ran1+ protein kinase and cAMP dependent protein kinase as negative regulators of fission yeast meiosis.
|
|
pubmed:affiliation |
Cold Spring Harbor Laboratory, NY 11724.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
