Molecular cloning and functional expression of a protein-serine/threonine phosphatase from the hyperthermophilic archaeon Pyrodictium abyssi TAG11.
An open reading frame coding for a putative protein-serine/threonine phosphatase was identified in the hyperthermophilic archaeon Pyrodictium abyssi TAG11 and named Py-PP1. Py-PP1 was expressed in Escherichia coli, purified from inclusion bodies, and biochemically characterized. The phosphatase gene is part of an operon which may provide, for the first time, insight into a physiological role for archaeal protein phosphatases in vivo.
Mai
B
B
Lehrstuhl für Mikrobiologie, Universität Regensburg, 93053 Regensburg, Germany.
Frey
G
G
Swanson
R V
RV
Mathur
E J
EJ
Stetter
K O
KO
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D019620:Desulfurococcaceae / Q000201:enzymology / Q000235:genetics*; D004926:Escherichia coli; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D010749:Phosphoprotein Phosphatases / Q000235:genetics* / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism; D017510:Protein Folding; D011994:Recombinant Proteins / Q000302:isolation & purification; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D010750:Phosphoproteins; D011994:Recombinant Proteins; C113952:Py-PP1 protein, Pyrodictium abyssi; D010749:Phosphoprotein Phosphatases