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rdf:type |
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lifeskim:mentions |
umls-concept:C0002085,
umls-concept:C0017337,
umls-concept:C0026255,
umls-concept:C0033640,
umls-concept:C0596988,
umls-concept:C0872306,
umls-concept:C1413253,
umls-concept:C1457869,
umls-concept:C1527180,
umls-concept:C1549081,
umls-concept:C1692758
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pubmed:issue |
2
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pubmed:dateCreated |
1996-8-5
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pubmed:databankReference |
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pubmed:abstractText |
LTE1 encodes a homolog of GDP-GTP exchange factors for the Ras superfamily and is required at low temperatures for cell cycle progression at the stage of the termination of M phase in Saccharomyces cerevisiae. We isolated extragenic suppressors which suppress the cold sensitivity of lte1 cells and confer a temperature-sensitive phenotype on cells. Cells mutant for the suppressor alone were arrested at telophase at non-permissive temperatures and the terminal phenotype was almost identical to that of lte1 cells at non-permissive temperatures. Genetic analysis revealed that the suppressor is allelic to CDC15, which encodes a protein kinase. The cdc15 mutations thus isolated were recessive with regard to the temperature-sensitive phenotype and were dominant with respect to suppression of lte1. We isolated CDC14 as a low-copy-number suppressor of cdc15-rlt1. CDC14 encodes a phosphotyrosine phosphatase (PTPase) and is essential for termination of M phase. An extra copy of CDC14 suppressed the temperature sensitivity of cdc15-rlt1 cells, but not that of cdc15-1 cells. In addition, some residues that are essential for the CDC14 PTPase activity were found to be non-essential for the suppression. These results strongly indicate that Cdc14 possesses dual functions; PTPase activity is needed for one function but not for the other. We postulate that the cooperative action of Cdc14 and Cdc15 plays an essential role in the termination of M phase.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDC14 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/CDC15 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/LTE1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0026-8925
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
251
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
176-85
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8668128-Alleles,
pubmed-meshheading:8668128-Amino Acid Sequence,
pubmed-meshheading:8668128-Base Sequence,
pubmed-meshheading:8668128-Binding Sites,
pubmed-meshheading:8668128-Cell Cycle Proteins,
pubmed-meshheading:8668128-DNA Primers,
pubmed-meshheading:8668128-Fungal Proteins,
pubmed-meshheading:8668128-GTP-Binding Proteins,
pubmed-meshheading:8668128-Gene Expression Regulation, Fungal,
pubmed-meshheading:8668128-Genes, Dominant,
pubmed-meshheading:8668128-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:8668128-Mitosis,
pubmed-meshheading:8668128-Molecular Sequence Data,
pubmed-meshheading:8668128-Phenotype,
pubmed-meshheading:8668128-Protein Kinases,
pubmed-meshheading:8668128-Protein Tyrosine Phosphatases,
pubmed-meshheading:8668128-Saccharomyces cerevisiae,
pubmed-meshheading:8668128-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8668128-Sequence Homology, Amino Acid,
pubmed-meshheading:8668128-Suppression, Genetic
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pubmed:year |
1996
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pubmed:articleTitle |
Dominant mutant alleles of yeast protein kinase gene CDC15 suppress the lte1 defect in termination of M phase and genetically interact with CDC14.
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pubmed:affiliation |
Department of Biological Sciences, Graduate School of Science, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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