A fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases

Sabine Ottilie, Jonathan Chernoff, Gerhard Hannig, Charles S. Hoffman, R. L. Erikson

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

Degenerate oligonucleotide probes encoding sequences conserved among mammalian protein-tyrosine-phosphatases (PTPases) were used to amplify DNA fragments from a Schizosaccharomyces pombe cDNA library by polymerise chain reaction (PCR) methods. A cloned PCR product predicted peptide sequences similar to those found in PTPases but not identical to any published sequences. A S. pombe gene, designated pyp1+, was identified in a cDNA library with this PCR probe, cloned, and sequenced. The sequence of the gene predicted a 550-amino acid protein with Mr 61,586, which includes amino acid sequences that are highly conserved in mammalian PTPases. Disruption of the pyp1+ gene resulted in viable cells. Overexpression of the pyp1+ gene in S. pombe permitted detection of a protein of apparent Mr 63,000.

Original languageEnglish
Pages (from-to)3455-3459
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number8
StatePublished - 1991

Keywords

  • Cell cycle control
  • Conserved sequences
  • Schizosaccharomyces pombe
  • Tyrosine phosphorylation

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