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J Biol Chem, Vol. 274, Issue 15, 10039-10046, April 9, 1999
From the The structural gene for a putative PPP family
protein-serine/threonine phosphatase from the microcystin-producing
cyanobacterium Microcystis aeruginosa PCC 7820, pp1-cyano1, was cloned. The sequence of the predicted gene
product, PP1-cyano1, was 98% identical to that of the predicted
product of an open reading frame, pp1-cyano2, from a
cyanobacterium that does not produce microcystins, M. aeruginosa UTEX 2063. By contrast, PP1-cyano1 displayed less than
20% identity with other PPP family protein phosphatases from
eukaryotic, archaeal, or other bacterial organisms. PP1-cyano1 and
PP1-cyano2 were expressed in Escherichia coli and purified
to homogeneity. Both enzymes exhibited divalent metal dependent
phosphohydrolase activity in vitro toward phosphoserine-
and phosphotyrosine-containing proteins and 3-phosphohistidine- and
phospholysine-containing amino acid homopolymers. This
multifunctional potential also was apparent in samples of PP1-cyano1
and PP1-cyano2 isolated from M. aeruginosa. Catalytic
activity was insensitive to okadaic acid or the cyanobacterially produced cyclic heptapeptide, microcystin-LR, both potent inhibitors of
mammalian PP1 and PP2A. PP1-cyano1 and PP1-cyano2 displayed diadenosine
tetraphosphatase activity in vitro. Diadenosine
tetraphosphatases share conserved sequence features with PPP family
protein phosphatases. The diadenosine tetraphosphatase activity of
PP1-cyano1 and PP1-cyano2 confirms that these enzymes share a common
catalytic mechanism.
Cyanobacterial PPP Family Protein Phosphatases Possess
Multifunctional Capabilities and Are Resistant to Microcystin-LR
,
Department of Biochemistry, Virginia
Polytechnic Institute and State University, Blacksburg, Virginia 24061 and the § Department of Biological Sciences, Wright State
University, Dayton, Ohio 45435
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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