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J Biol Chem, Vol. 274, Issue 11, 6992-7001, March 12, 1999
From the Department of Molecular Genetics and Microbiology, State
University of New York at Stony Brook,
Stony Brook, New York 11794-5222
The highly conserved non-structural protein 2C of
picornaviruses is involved in viral genome replication and
encapsidation and in the rearrangement of intracellular structures. 2C
binds RNA, has nucleoside triphosphatase activity, and shares three motifs with superfamily III helicases. Motifs "A" and "B" are involved in nucleotide triphosphate (NTP) binding and hydrolysis, whereas a function for motif "C" has not yet been demonstrated. Poliovirus RNA replication is inhibited by millimolar concentrations of
guanidine hydrochloride (GdnHCl). Resistance and dependence to GdnHCl
map to 2C. To characterize the nucleoside triphosphatase activity of
2C, we purified poliovirus recombinant 2C fused to glutathione
S-transferase (GST-2C) from Escherichia coli.
GST-2C hydrolyzed ATP with a Km of 0.7 mM. Other NTPs, including GTP, competed with ATP for
binding to 2C but were poor substrates for hydrolysis. Mutation of
conserved residues in motif A and B abolished ATPase activity, as did
mutation of the conserved asparagine residue in motif C, an observation
indicating the involvement of this motif in ATP hydrolysis. GdnHCl at
millimolar concentrations inhibited ATP hydrolysis. Mutations in 2C
that confer poliovirus resistant to or dependent on GdnHCl increased
the tolerance to GdnHCl up to 100-fold.
Characterization of the Nucleoside Triphosphatase Activity of
Poliovirus Protein 2C Reveals a Mechanism by Which Guanidine Inhibits
Poliovirus Replication
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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