title: Gene cloning and expression and characterization of a toxin-sensitive protein phosphatase from the methanogenic archaeon Methanosarcina thermophila TM-1.
abstract: With oligonucleotides modelled after conserved regions within the protein-serine/threonine phosphatases (PPs) of the PP1/2A/2B superfamily, the gene for the archaeal protein phosphatase PP1-arch2 was identified, cloned, and sequenced from the methanogenic archaeon Methanosarcina thermophila TM-1. The DNA-derived amino acid sequence of PP1-arch2 exhibited a high degree of sequence identity, 27 to 31%, with members of the PP1/2A/2B superfamily such as PP1-arch1 from Sulfolobus solfataricus, PP1alpha from rats, PP2A from Saccharomyces cerevisiae, and PP2B from humans. The activity of the recombinant PP1-arch2 was sensitive to several naturally occurring microbial toxins known to potently inhibit eucaryal PP1 and PP2A, including microcystin-LR, okadaic acid, tautomycin, and calyculin A.
authors.affiliation: Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308, USA.
authors.forename: B
authors.initials: B
authors.lastname: Solow
authors.forename: J C
authors.initials: JC
authors.lastname: Young
authors.forename: P J
authors.initials: PJ
authors.lastname: Kennelly
mesh_terms: D000085:Acetates / Q000378:metabolism; D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D015870:Gene Expression; D005798:Genes, Bacterial; D017020:Methanosarcina / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D010768:Phosphoserine / Q000378:metabolism; D019000:Phosphotyrosine / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D000085:Acetates; D011994:Recombinant Proteins; D010768:Phosphoserine; D019000:Phosphotyrosine; D010749:Phosphoprotein Phosphatases