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Interaction of nucleoredoxin with protein phosphatase 2A
Author(s) -
Lechward Katarzyna,
Sugajska Ewa,
de Baere Ivo,
Goris Jozef,
Hemmings Brian A.,
Zolnierowicz Stanislaw
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.04.101
Subject(s) - chemistry , phosphatase , biochemistry , enzyme
A trimeric protein phosphatase 2A (PP2A T55 ) composed of the catalytic (PP2Ac), structural (PR65/A), and regulatory (PR55/B) subunits was isolated from rabbit skeletal muscle by thiophosphorylase affinity chromatography, and contained two additional proteins of 54 and 55 kDa, respectively. The 54 kDa protein was identified as eukaryotic translation termination factor 1 (eRF1) and as a PP2A interacting protein [Andjelkovic et al. (1996) EMBO J. 15, 101–112]. The 55 kDa protein is now identified as nucleoredoxin (NRX). The formation of a complex between GST–NRX, PP2A C and PP2A D was demonstrated by pull‐down experiments with purified forms of PP2A, and by immunoprecipitation of HA‐tagged NRX expressed in HEK293 cells complexed endogenous PP2A subunits. Analysis of PP2A activity in the presence of GST–NRX showed that NRX competed with polycations for both stimulatory and inhibitory effects on different forms of PP2A.