Conserved aspartic acid 233 and alanine 231 are not required for poliovirus polymerase function in replicons.
Nucleic acid polymerases have similar structures and motifs. The function of an aspartic acid (conserved in all classes of nucleic acid polymerases) in motif A remains poorly understood in RNA-dependent RNA polymerases. We mutated this residue to alanine in a poliovirus replicon. The resulting mutant could still replicate, although at a reduced level. In addition, mutation A231C (also in motif A) yielded high levels of replication. Taken together these results show that poliovirus polymerase conserved residues D233 and A231 are not essential to poliovirus replicon function.
Freistadt
Marion S
MS
Department of Microbiology, Immunology and Parasitology, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112, USA. mfreis@tulane.edu
Eberle
Karen E
KE
D000409:Alanine / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001224:Aspartic Acid / Q000737:chemistry; D001483:Base Sequence; D017124:Conserved Sequence; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D017955:Poliovirus / Q000201:enzymology / Q000235:genetics / Q000502:physiology*; D012324:RNA-Dependent RNA Polymerase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012093:Replicon / Q000235:genetics / Q000502:physiology*; D013329:Structure-Activity Relationship; D014779:Virus Replication
D001224:Aspartic Acid; D012324:RNA-Dependent RNA Polymerase; D000409:Alanine