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Vol. 13, Issue 10, 3477-3492, October 2002
Department of Biology, Syracuse University, Syracuse, New York
13244
Protein phosphatase 2A (PP2A) regulates a broad spectrum of
cellular processes. This enzyme is a collection of varied
heterotrimeric complexes, each composed of a catalytic (C) and
regulatory (B) subunit bound together by a structural (A) subunit. To
understand the cell cycle dynamics of this enzyme population, we
carried out quantitative and qualitative analyses of the PP2A subunits of Saccharomyces cerevisiae. We found the following: the
level of each subunit remained constant throughout the cell cycle;
there is at least 10 times more of one of the regulatory subunits
(Rts1p) than the other (Cdc55p); Tpd3p, the structural subunit, is
limiting for both catalytic and regulatory subunit binding. Using green fluorescent protein-tagged forms of each subunit, we monitored the
sites of significant accumulation of each protein throughout the cell
cycle. The two regulatory subunits displayed distinctly different
dynamic localization patterns that overlap with the A and C subunits at
the bud tip, kinetochore, bud neck, and nucleus. Using
strains null for single subunit genes, we confirmed the hypothesis that
regulatory subunits determine sites of PP2A accumulation. Although
Rts1p and Tpd3p required heterotrimer formation to achieve normal
localization, Cdc55p achieved its normal localization in the absence of
either an A or C subunit.
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