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Comparison of the biochemical and biological functions of tyrosine phosphatases from fission yeast, budding yeast and animal cells
Author(s) -
Hannig Gerhard,
Ottilie Sabine,
Schievella Andrea R.,
Erikson Raymond L.
Publication year - 1993
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320091002
Subject(s) - biology , cdc25 , wee1 , protein tyrosine phosphatase , saccharomyces cerevisiae , yeast , phosphatase , mutant , microbiology and biotechnology , mitosis , gene , tyrosine , genetics , cell cycle , biochemistry , cyclin dependent kinase 1 , phosphorylation
Abstract In a previous communication, we have shown that two protein tyrosine phosphatases (PTPases) from fission yeast, pyp1 + and pyp2 + , act as novel inhibitors of mitosis upstream of the wee1 + lmik1 + pathway (Ottilie et al. , 1992). Here we describe that both genes possess intrinsic PTPase activity as judged by in vitro PTPase assays using 32 P‐labeled Raytide as a substrate, and that 32 P‐labeled p107 wee1 is an in vitro substrate for pyp1. To compare the biological activity of pyp1 and pyp2 to that of other known PTPases, we expressed the budding yeast PTP1 and human placental phosphatase 1B ( PTP1B ) genes in either a cdc25–22 or wee1–50 genetic background and established that, in contrast to pyp1 + and pyp2 + , Saccharomyces cerevisiae PTP1 and human PTP1B complement the cdc25 mutant, opposing the wee1 + lmik1 + pathway.