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J Biol Chem, Vol. 273, Issue 18, 11241-11247, May 1, 1998
From the Departments of Molecular Microbiology and Medicine, Howard
Hughes Medical Institute, Washington University School of Medicine,
St. Louis, Missouri 63110
We have cloned a gene from Plasmodium
falciparum with homology to the
Mg2+-dependent serine/threonine protein
phosphatase 2C (PP2C) family. The predicted coding region is 920 amino
acids long, twice the size of other members of this family. We show
that this protein can be divided into two halves (Pf2C-1 and
Pf2C-2), each a complete phosphatase unit with homology to other
phosphatases of this class. To study the function of this PP2C, we have
tested the ability of different constructs to complement conditional
null mutants of yeast. Our results show that expression of the
full-length protein, the first half alone, the second half alone, or a
hybrid with the N terminus of the first half and the C terminus of the second half was able to complement the heat shock response defect of a
Schizosaccharomyces pombe strain with a PP2C
(PTC1) deletion. Recombinant P. falciparum PP2C
expressed in Escherichia coli was active in
dephosphorylating 32P-labeled casein in an
Mg2+- or Mn2+-dependent reaction.
Each half alone was also active in recombinant form. Using the
two-hybrid system, we have shown that the two halves can interact. Gel
filtration assay of P. falciparum protein extracts suggests
that full-length PfPP2C is a dimer, and phosphatase activity
competition experiments indicate that dimerization of PfPP2C is
required for its optimal activity. This unusual phosphatase molecule
appears to be composed of four catalytic units on two polypeptide
chains.
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