Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1752, Issue 2, Pages 133-141Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2005.07.021
Keywords
plant; Arabidopsis thaliana; antisense fibroblast growth factor; GFG protein; nudix hydrolase; ADP-ribose
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In a search for a plant antimutator MutT protein, an Arabidopsis thaliana Nudix hydrolase with homology to the mammalian GFG protein was expressed as a hexahistidine fusion polypeptide in Escherichia coli and purified to homogeneity. Unlike the GFG protein, the A. thaliana homolog could not complement the mutT mutation in a Muff-deficient E. coli strain nor was it able to hydrolyze 8-oxo-dGTP, the main substrate of the Muff protein. Instead the recombinant protein hydrolyzed a variety of nucleoside diphosphate derivatives showing a preference for ADP-ribose, with K-m and k(cat) values of 1.2 mM and 2.7 s(-1) respectively. The products of ADP-ribose hydrolysis were AMP and ribose-5-phosphate. The optimal activity was at alkaline pH (8.5) with Mg2+ (5 mM) ions as the cofactor. The protein exists as a dimmer in solution. (C) 2005 Elsevier B.V. All rights reserved.
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