Booher, R., Beach, D. (June 1989) Involvement of a type 1 protein phosphatase encoded by bws1+ in fission yeast mitotic control. Cell, 57 (6). pp. 1009-16. ISSN 1097-4172
Abstract
Fission yeast cdc25+ and wee1+ interact genetically with cdc2+ in the regulation of cell division, respectively as a mitotic activator and inhibitor. cdc25+ is normally essential for mitosis, but this requirement is alleviated in a loss-of-function wee1 mutant background. A plasmid-borne sequence, other than wee1+, that causes a cdc25ts wee1- double mutant to revert to a temperature-sensitive cdc phenotype has been isolated. The gene carried by this plasmid is called bws1+ (for bypass of wee suppression). bws1+ also bypasses the ability of alleles of cdc2 that confer a wee phenotype (cdc2w) to suppress loss-of-function cdc25 mutants. The nucleotide sequence of bws1+ shows that the predicted protein shares 81% amino acid identity with the catalytic subunit of mammalian type 1 protein phosphatase. Thus a genetic screen that might have yielded a protein kinase (wee1+) uncovered a phosphatase that also appears to be involved in the pathway of mitotic control.
Item Type: | Paper |
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Uncontrolled Keywords: | Alleles Amino Acid Sequence Aspergillus Nuclease S1 Base Sequence Cloning, Molecular Endonucleases/pharmacology Fungal Proteins/genetics *Genes, Fungal Genes, Lethal *Mitosis Molecular Sequence Data Mutation Phenotype Phosphoprotein Phosphatase/*genetics Research Support, U.S. Gov't, P.H.S. Saccharomycetales/*genetics Schizosaccharomyces/*genetics Transcription, Genetic |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > Mitogen-activated protein kinase bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein phosphatase |
CSHL Authors: | |
Communities: | CSHL labs > Beach lab |
Depositing User: | Gail Sherman |
Date: | 16 June 1989 |
Date Deposited: | 28 Jul 2017 16:51 |
Last Modified: | 28 Jul 2017 16:51 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/34832 |
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