title: Investigation of activity of recombinant mengovirus RNA-dependent RNA polymerase and its mutants.
abstract: The activities of wild-type mengovirus RNA polymerase (RdRP) and of its three mutants with C-terminal tryptophan residue replaced by residues of alanine (W460A), phenylalanine (W460F), or tyrosine (W460Y) were studied. The proteins were expressed in E. coli and purified by affinity chromatography with the IMPACT system. The isolated recombinant proteins were studied using a cell-free replication system on elongation of oligo(U) primer on RNA template corresponding to the 3'-terminal 366-meric fragment of the mengovirus RNA. The activities of the mutant polymerases were comparable to that of the wild-type enzyme.
authors: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russia. barsa19@rambler.ru
authors: G S
authors: GS
authors: Shatskaya
authors: V L
authors: VL
authors: Drutsa
authors: O N
authors: ON
authors: Koroleva
authors: I A
authors: IA
authors: Osterman
authors: T M
authors: TM
authors: Dmitrieva
mesh_terms: D008574:Mengovirus / Q000201:enzymology*; D050505:Mutant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D009154:Mutation; D012324:RNA-Dependent RNA Polymerase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D050505:Mutant Proteins; D011994:Recombinant Proteins; D012324:RNA-Dependent RNA Polymerase