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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1991-8-19
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pubmed:databankReference |
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pubmed:abstractText |
To study the regulation of tyrosine phosphorylation/dephosphorylation in Saccharomyces cerevisiae, a protein tyrosine phosphatase (PTPase) was cloned by the polymerase chain reaction (PCR). Conserved amino acid sequences within the mammalian PTPases were used to design primers which generated a yeast PCR fragment. The sequence of the PCR fragment encoded a protein with homology to the mammalian PTPases. The PCR fragment was used to identify the yeast PTP1 gene which has an open reading frame encoding a 335-amino acid residue protein. This yeast PTPase shows 26% sequence identity to the rat PTPase, although highly conserved residues within the mammalian enzymes are invariant in the yeast protein. The yeast PTP1 is physicallt linked to the 5'-end of a heat shock gene SSB1. This yeast PTP1 gene was expressed in Escherichia coli and obtained in a highly purified form by a single affinity chromatography step. The recombinant yeast PTPase hydrolyzed phosphotyrosine containing substrates approximately 1000 times faster than a phosphoserine containing substrate. Gene disruption of yeast PTP1 has no visible effect on vegetative growth.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12964-70
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1649172-Amino Acid Sequence,
pubmed-meshheading:1649172-Base Sequence,
pubmed-meshheading:1649172-Cloning, Molecular,
pubmed-meshheading:1649172-Genes, Fungal,
pubmed-meshheading:1649172-Kinetics,
pubmed-meshheading:1649172-Molecular Sequence Data,
pubmed-meshheading:1649172-Oligonucleotide Probes,
pubmed-meshheading:1649172-Phosphoprotein Phosphatases,
pubmed-meshheading:1649172-Polymerase Chain Reaction,
pubmed-meshheading:1649172-Protein Tyrosine Phosphatases,
pubmed-meshheading:1649172-Recombinant Proteins,
pubmed-meshheading:1649172-Restriction Mapping,
pubmed-meshheading:1649172-Saccharomyces cerevisiae,
pubmed-meshheading:1649172-Sequence Homology, Nucleic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
Cloning and expression of a yeast protein tyrosine phosphatase.
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pubmed:affiliation |
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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