{'fraction_non_alphanumeric': 0.03368421052631579, 'fraction_numerical': 0.03894736842105263, 'mean_word_length': 5.256578947368421, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Comparison of the biochemical and biological functions of tyrosine phosphatases from fission yeast, budding yeast and animal cells

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 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+ lmik1+ pathway.