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J. Biol. Chem., Vol. 269, Issue 45, 27996-27999, Nov, 1994
O Mondesert, S Moreno and P Russell
Cdc25 protein phosphatase dephosphorylates tyrosine 15 of Cdc2, thereby
activating Cdc2/cyclin B kinase, which then brings about mitosis. A fission
yeast (Schizosaccharomyces pombe) cDNA expression library was screened for
clones that rescue cdc25-22. In addition to the cdc25+ and pyp3+
protein-tyrosine phosphatase genes, a third gene was discovered. This gene,
named stp1+ (small tyrosine phosphatase), encodes a approximately 17.5-kDa
protein that is approximately 42% identical to members of an unusual class
of small (approximately 18 kDa) cytosolic phosphatases previously known to
exist only in mammalian species. The biological functions of these proteins
are unknown, but they have vigorous protein-tyrosine phosphatase activity
in vitro and have a sequence motif, Cys-X5-Arg, that is present at the
active sites of all known types of protein-tyrosine phosphatases. Sequence
homology between S. pombe Stp1 and its mammalian homologs is particularly
high in the active site region of the proteins. Rescue of cdc25-22 by
overproduction of Stp1 protein is probably due to an ability of Stp1 to
dephosphorylate tyrosine 15 of Cdc2. Disruption of stp1+ causes no obvious
phenotype. The fact that Stp1 homologs are highly conserved between yeast
and man suggests that they have important functions.
Low molecular weight protein-tyrosine phosphatases are highly conserved between fission yeast and man
Department of Molecular and Cell Biology MB-3, Scripps Research Institute, La Jolla, California 92037.
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