Identification of Protein-Tyrosine Phosphatases in Archaea |
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Authors: | Dimitrios J Stravopodis Nikos C Kyrpides |
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Institution: | (1) St. Jude Children's Research Hospital, Department of Biochemistry, 332 N. Lauderdale, Memphis TN 38105, USA, US;(2) Department of Microbiology, University of Illinois at Urbana–Champaign, 407 S. Goodwin Avenue, Urbana IL 61801, USA, US |
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Abstract: | Protein-tyrosine dephosphorylation is a major mechanism in cellular regulation. A large number of protein-tyrosine phosphatases
is known from Eukarya, and more recently bacterial homologues have also been identified. By employing conserved sequence patterns
from both eukaryotic and bacterial protein-tyrosine phosphatases, we have identified three homologous sequences in two of
the four complete archaeal genomes. Two hypothetical open reading frames in the genome of Methanococcus jannaschii (MJ0215 and MJECL20) and one in the genome of Pyrococcus horikoshii (PH1732) clearly bear all the conserved residues of this family. No homologues were found in the genomes of Archaeoglobus fulgidus and Methanobacterium thermoautotrophicum. This is the first report of protein-tyrosine phosphatase sequences in Archaea.
Received: 29 April 1998 / Accepted: 27 November 1998 |
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Keywords: | : Protein-tyrosine phosphatases — Archaea |
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