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Analysis by in vitro mutagenesis of PP2A alpha okadaic acid responsive sequences.

Abstract：

:It has been shown that the protein serine/threonine phosphatase type 2A alpha catalytic subunit (PP2A alpha) has a mutation consisting of a glycine substitution for cysteine at 269 in the okadaic acid resistant variant of CHO cells, and that the mutant protein is resistant to okadaic acid (Shima, H. et al. Proc. Natl. Acad. Sci. USA 91, 9267-9271, 1994). In this study we analyzed okadaic acid responsive sequences in PP2A alpha by introducing a mutation at around codon 269 of the cDNA strand. The recombinant mutant PP2A alpha proteins Y265F, C266G, Y267G and C269Y were resistant to okadaic acid, with IC50s of 10, 24, 20 and 10 nM, respectively, as opposed to the recombinant wild PP2A alpha protein which had an IC50 of 0.24 nM. This observation suggests that not only cysteine at 269, but also other YCY amino acids, between 265-267, are necessary for the high sensitivity of PP2A to okadaic acid.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kaneko S,Shima H,Amagasa T,Takagi M,Sugimura T,Nagao M

doi

10.1006/bbrc.1995.2317

subject

Has Abstract

pub_date

1995-09-14 00:00:00

pages

518-23

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)72317-0

journal_volume

214

pub_type

杂志文章

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