Comparison of the biochemical and biological functions of tyrosine phosphatases from fission yeast, budding yeast and animal cells
| Autor: | Gerhard Hannig, Raymond L. Erikson, Sabine Ottilie, Andrea R. Schievella |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Cdc25
Placenta Saccharomyces cerevisiae Phosphatase Molecular Sequence Data Mitosis Bioengineering Protein tyrosine phosphatase Biology Applied Microbiology and Biotechnology Biochemistry Gene Expression Regulation Fungal Schizosaccharomyces Genetics Humans Tyrosine Phosphorylation Base Sequence Genetic Complementation Test biology.organism_classification Yeast Wee1 Schizosaccharomyces pombe Mutation biology.protein Protein Tyrosine Phosphatases Biotechnology |
| Zdroj: | Yeast (Chichester, England). 9(10) |
| ISSN: | 0749-503X |
| Popis: | In a previous communication, we have shown that two protein tyrosine tyrosine phosphatases (PTPases) from fission yeast, pyp1+ and pyp2+, act as novel inhibitors of mitosis upstream of the wee1+/mik1+ pathway (Ottilie et al., 1992). Here we describe that both genes possess intrinsic PTPase activity as judged by in vitro PTPase assays using 32P-labeled Raytide as a substrate, and that 32P-labeled p107wee1 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+/mik1+ pathway. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text