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Papers In Press, published online ahead of print March 16, 2006
Queensland Cancer Fund Research Laboratory, Queensland Institute of Medical Research, Brisbane, Qld 4029
Corresponding Author: martinL{at}qimr.edu.au
Aprataxin hydrolyses, with similar efficiency, the model Histidine triad nucleotide binding Ataxia with oculomotor apraxia type 1 (AOA1) is an early onset autosomal recessive spinocerebellar ataxia with a defect in the protein Aprataxin, implicated in the response of cells to DNA damage. We describe here the expression of a recombinant form of Aprataxin and show that it has dual DNA binding and nucleotide hydrolase activities. This protein binds to double stranded DNA with high affinity, but is also capable of binding double stranded RNA and single strand DNA, with preferential binding to hairpin structures. No increased binding was observed with a variety of DNA structures mimicking intermediates in DNA repair. The DNA binding observed here was not dependent on zinc and addition of exogenous zinc abolished DNA binding. We also demonstrate that protein substrate, AMPNH2 and the Fragile histidine triad protein substrate, Ap4A. These activities were significantly reduced in the presence of duplex DNA and to a lesser extent in the presence of single strand DNA. Finally, comparison of sequence relationships between the Histidine triad superfamily members, show that Aprataxin forms a distinct branch in this superfamily. In addition to its capacity for nucleotide binding and hydrolysis the observation that it also binds DNA and RNA adds a new dimension to this superfamily of proteins and provides further support for a role for Aprataxin in the cellular response to DNA damage.
J. Biol. Chem, 10.1074/jbc.M507946200
Submitted on July 21, 2005
Accepted on March 16, 2006
Aprataxin forms a discrete branch in the hit superfamily of proteins with both DNA/RNA binding and nucleotide hydrolase activities
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