[HTML][HTML] Functional expression of human PP2Ac in yeast permits the identification of novel C-terminal and dominant-negative mutant forms
DRH Evans, T Myles, J Hofsteenge… - Journal of Biological …, 1999 - ASBMB
The protein phosphatase 2A (PP2A) holoenzyme is structurally conserved among
eukaryotes. This reflects a conservation of function in vivo because the human catalytic
subunit (PP2Ac) functionally replaced the endogenous PP2Ac of Saccharomyces cerevisiae
and bound the yeast regulatory PR65/A subunit (Tpd3p) forming a dimer. Yeast was
employed as a novel system for mutagenesis and functional analysis of human PP2Ac,
revealing that the invariant C-terminal leucine residue, a site of regulatory methylation, is …
eukaryotes. This reflects a conservation of function in vivo because the human catalytic
subunit (PP2Ac) functionally replaced the endogenous PP2Ac of Saccharomyces cerevisiae
and bound the yeast regulatory PR65/A subunit (Tpd3p) forming a dimer. Yeast was
employed as a novel system for mutagenesis and functional analysis of human PP2Ac,
revealing that the invariant C-terminal leucine residue, a site of regulatory methylation, is …
