Investigation of activity of recombinant mengovirus RNA-dependent RNA polymerase and its mutants

G. S. Shatskaya, V. L. Drutsa, O. N. Koroleva, I. A. Osterman, T. M. Dmitrieva

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

The activities of wild-type mengovirus RNA polymerase (RdRP) and of its three mutants with C-terminal tryp-tophan 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.

Original languageEnglish
Pages (from-to)96-101
Number of pages6
JournalBiochemistry (Moscow)
Volume78
Issue number1
DOIs
Publication statusPublished - Jan 2013
Externally publishedYes

Keywords

  • IMPACT system
  • mengovirus
  • RNA-dependent RNA polymerase

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