A PPM-family protein phosphatase from the thermoacidophile Thermoplasma volcanium hydrolyzes protein-bound phosphotyrosine |
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Authors: | Hanan Dahche AbdulShakur Abdullah M Ben Potters Peter J Kennelly |
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Institution: | (1) Department of Biochemistry, Virginia Polytechnic Institute and State University, 111C Engel Hall, Blacksburg, VA 24061, USA |
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Abstract: | The genomes of virtually all free-living archaeons encode one or more deduced protein-serine/threonine/tyrosine kinases belonging
to the so-called eukaryotic protein kinase superfamily. However, the distribution of their cognate protein-serine/threonine/phosphatases
displays a mosaic pattern. Thermoplasma volcanium is unique among the Archaea inasmuch as it is the sole archaeon whose complement of deduced phosphoprotein phosphatases includes a member of the PPM-family
of protein-serine/threonine phosphatases—a family that originated in the Eucarya. A recombinant version of this protein, TvnPPM, exhibited protein-tyrosine phosphatase in addition to its predicted protein-serine/threonine
phosphatase activity in vitro. TvnPPM is the fourth member of the PPM-family shown to exhibit such dual-specific capability, suggesting that the ancestral
versions of this enzyme exhibited broad substrate specificity. Unlike most other archeaons, the genome of T. volcanium lacks open reading frames encoding stereotypical protein-tyrosine phosphatases. Hence, the dual-specificity of TvnPPM may
account for its seemingly aberrant presence in an archaeon. |
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Keywords: | Protein phosphorylation Signal transduction Dual-specific protein phosphatase Archaea Protein-tyrosine phosphatase Protein-serine/threonine phosphatase Zinc |
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