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J Biol Chem, Vol. 274, Issue 20, 14382-14391, May 14, 1999
From the Carboxymethylation of proteins is a highly
conserved means of regulation in eukaryotic cells. The protein
phosphatase 2A (PP2A) catalytic (C) subunit is reversibly methylated at
its carboxyl terminus by specific methyltransferase and methylesterase
enzymes which have been purified, but not cloned. Carboxymethylation
affects PP2A activity and varies during the cell cycle. Here, we report that substitution of glutamine for either of two putative active site
histidines in the PP2A C subunit results in inactivation of PP2A and
formation of stable complexes between PP2A and several cellular
proteins. One of these cellular proteins, herein named protein
phosphatase methylesterase-1 (PME-1), was purified and microsequenced,
and its cDNA was cloned. PME-1 is conserved from yeast to human and
contains a motif found in lipases having a catalytic triad-activated
serine as their active site nucleophile. Bacterially expressed PME-1
demethylated PP2A C subunit in vitro, and okadaic acid, a
known inhibitor of the PP2A methylesterase, inhibited this reaction. To
our knowledge, PME-1 represents the first mammalian protein
methylesterase to be cloned. Several lines of evidence indicate that,
although there appears to be a role for C subunit carboxyl-terminal
amino acids in PME-1 binding, amino acids other than those at the
extreme carboxyl terminus of the C subunit also play an important role
in PME-1 binding to a catalytically inactive mutant.
A Protein Phosphatase Methylesterase (PME-1) Is One of Several
Novel Proteins Stably Associating with Two Inactive Mutants of Protein
Phosphatase 2A
§,**,,**
Division of Cellular and Molecular Biology,
Dana-Farber Cancer Institute and Harvard Medical School, Boston,
Massachusetts 02115, the § Institute of Molecular Biology,
University of Vienna, A-1030 Vienna, Austria, the ** Department of
Biochemistry and Winship Cancer Center, Emory University School of
Medicine, Atlanta, Georgia 30322, and the
§§ Harvard Microchemistry Facility, Harvard
Biological Laboratories, Cambridge, Massachusetts 02138
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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