PMID: 8970981Dec 1, 1996Paper

Mutation of lysine residues in the nucleotide binding segments of the poliovirus RNA-dependent RNA polymerase

Journal of Virology
O C RichardsE Ehrenfeld

Abstract

The poliovirus 3D RNA-dependent RNA polymerase contains two peptide segments previously shown to cross-link to nucleotide substrates via lysine residues. To determine which lysine residue(s) might be implicated in catalytic function, we engineered mutations to generate proteins with leucine residues substituted individually for each of the lysine residues in the NTP binding regions. These proteins were expressed in Escherichia coli and were examined for their abilities to bind nucleotides and to catalyze RNA chain elongation in vitro. Replacement of each lysine residue in the NTP binding segment located in the central portion of the 3D molecule (Lys-276, -278, or -283) with leucine produced no impairment of GTP binding or polymerase activity. Substitution of leucine for Lys-61 in the N-terminal portion of the protein, however, abolished the binding of protein to GTP-agarose and all detectable polymerase activity. A nearby lysine replacement with leucine at position 66 had no effect on enzyme activity. The three mutations in the central region of 3D were introduced into full-length viral cDNAs, and the infectivities of RNA transcripts were examined in transfected HeLa cells. Growth of virus containing 3D with a mutation at resid...Continue Reading

References

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Citations

Sep 12, 1997·The Journal of Biological Chemistry·O C Richards, E Ehrenfeld
Apr 15, 2003·Journal of Virology·Shane CrottyRaul Andino
Apr 10, 1999·The Journal of Biological Chemistry·V LohmannR Bartenschlager

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