Catalytic domains of the LAR and CD45 protein tyrosine phosphatases from Escherichia coli expression systems: purification and characterization for specificity and mechanism

Biochemistry ◽  
1992 ◽  
Vol 31 (1) ◽  
pp. 133-138 ◽  
Author(s):  
Hyeongjin Cho ◽  
Shawn E. Ramer ◽  
Michiyasu Itoh ◽  
Eric Kitas ◽  
Willi Bannwarth ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Tyrosine Phosphatases ◽  
Expression Systems ◽  
Tyrosine Phosphatases ◽  
Purification And Characterization ◽  
Protein Tyrosine ◽  
Catalytic Domains ◽  
Escherichia Coli Expression

The fission yeast genes pyp1+ and pyp2+ encode protein tyrosine phosphatases that negatively regulate mitosis

1992 ◽  
Vol 12 (12) ◽  
pp. 5571-5580
Author(s):  
S Ottilie ◽  
J Chernoff ◽  
G Hannig ◽  
C S Hoffman ◽  
R L Erikson
Keyword(s):  
Synthetic Lethality ◽  
Protein Tyrosine Phosphatases ◽  
Temperature Sensitive ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Catalytic Domains ◽  
C Terminus ◽  
Degenerate Oligonucleotide ◽  
Genes Encoding ◽  
Yeast Genes

We have used degenerate oligonucleotide probes based on sequences conserved among known protein tyrosine phosphatases (PTPases) to identify two Schizosaccharomyces pombe genes encoding PTPases. We previously described the cloning of pyp1+ (S. Ottilie, J. Chernoff, G. Hannig, C. S. Hoffman, and R. L. Erikson, Proc. Natl. Acad. Sci. USA 88:3455-3459, 1991), and here we describe a second gene, called pyp2+. The C terminus of each protein contains sequences conserved in the apparent catalytic domains of all known PTPases. Disruption of pyp2+ results in viable cells, as was the case for pyp1+, whereas disruption of pyp2+ and pyp1+ results in synthetic lethality. Overexpression of either pyp1+ or pyp2+ in wild-type strains leads to a delay in mitosis but is suppressed by a wee1-50 mutation at 35 degrees C or a cdc2-1w mutation. A pyp1 disruption suppresses the temperature-sensitive lethality of a cdc25-22 mutation. Our data suggest that pyp1+ and pyp2+ act as negative regulators of mitosis upstream of the wee1+/mik1+ pathway.

scholarly journals The fission yeast genes pyp1+ and pyp2+ encode protein tyrosine phosphatases that negatively regulate mitosis.

1992 ◽  
Vol 12 (12) ◽  
pp. 5571-5580 ◽  
Author(s):  
S Ottilie ◽  
J Chernoff ◽  
G Hannig ◽  
C S Hoffman ◽  
R L Erikson
Keyword(s):  
Synthetic Lethality ◽  
Protein Tyrosine Phosphatases ◽  
Temperature Sensitive ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Catalytic Domains ◽  
C Terminus ◽  
Degenerate Oligonucleotide ◽  
Genes Encoding ◽  
Yeast Genes

We have used degenerate oligonucleotide probes based on sequences conserved among known protein tyrosine phosphatases (PTPases) to identify two Schizosaccharomyces pombe genes encoding PTPases. We previously described the cloning of pyp1+ (S. Ottilie, J. Chernoff, G. Hannig, C. S. Hoffman, and R. L. Erikson, Proc. Natl. Acad. Sci. USA 88:3455-3459, 1991), and here we describe a second gene, called pyp2+. The C terminus of each protein contains sequences conserved in the apparent catalytic domains of all known PTPases. Disruption of pyp2+ results in viable cells, as was the case for pyp1+, whereas disruption of pyp2+ and pyp1+ results in synthetic lethality. Overexpression of either pyp1+ or pyp2+ in wild-type strains leads to a delay in mitosis but is suppressed by a wee1-50 mutation at 35 degrees C or a cdc2-1w mutation. A pyp1 disruption suppresses the temperature-sensitive lethality of a cdc25-22 mutation. Our data suggest that pyp1+ and pyp2+ act as negative regulators of mitosis upstream of the wee1+/mik1+ pathway.

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