Purification of plant protein phosphatase PP7 and evidence for its redox regulation

被引：5

作者：

Andreeva, AV

Solov'eva, OV

Kakuev, DL

Kutuzov, MA

机构：

[1] Oxford Brookes Univ, Res Sch Biol & Mol Sci, Oxford OX3 0BP, England

[2] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Lab Prot Hormonal Regulat, Moscow 117871, Russia

[3] CEA Grenoble, Dept Biol Mol & Struct, Lab Biophys Mol & Cellulaire, F-38054 Grenoble, France

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2001年 / 396卷 / 01期

基金：

俄罗斯基础研究基金会;

关键词：

protein phosphorylation; protein Ser/Thr phosphatase; PP7; purification; redox; thiol-disulfide exchange; Arabidopsis thaliana;

D O I：

10.1006/abbi.2001.2582

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

PP7, a recently identified protein Ser/Thr phosphatase of the PPP family distantly related to phosphatases PP5/PPT and PPEF/rdgC, was purified from cauliflower extracts to apparent homogeneity. Purified cauliflower PP7 and recombinant PP7 expressed in Escherichia coli exhibit light absorption in the visible range with a maximum at similar to 430 nm. Under nonreducing conditions, native PP7 exists as a mixture of monomer with an intramolecular disulfide bridge, disulfide-linked homodimer, and possibly disulfide-linked complexes with potential partner proteins. The activity of recombinant Arabidopsis thaliana PP7 is reversibly regulated by redox agents. The results demonstrate the existence of PP7 protein in planta and suggest a possibility of redox regulation of this protein phosphatase. (C) 2001 Elsevier Science.

引用

页码：65 / 70

页数：6

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[11] Characterization and possible redox regulation of the purified calmodulin-dependent NAD+ kinase from Lycopersicon pimpinellifolium [J].