Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses. - PubMed - NCBI
Virology. 2015 Jun 11;484:80-85. doi: 10.1016/j.virol.2015.05.016. [Epub ahead of print]
Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses.
Abstract
Enteroviruses (EV) uridylylate a peptide, VPg, as the first step in their replication. VPgpUpU, found free in infected cells, serves as the primer for RNA elongation. The abilities of four polymerases (3Dpol), from EV-species A-C, to uridylylate VPgs that varied by up to 60% of their residues were compared. Each 3Dpol was able to uridylylate all five VPgs using polyA RNA as template, while showing specificity for its own genome encoded peptide. All 3Dpol uridylylated a consensus VPg representing the physical chemical properties of 31 different VPgs. Thus the residues required for uridylylation and the enzymatic mechanism must be similar in diverse EV. As VPg-binding sites differ in co-crystal structures, the reaction is probably done by a second 3Dpol molecule. The conservation of polymerase residues whose mutation reduces uridylylation but not RNA elongation is compared. Copyright © 2015 Elsevier Inc. All rights reserved.
KEYWORDS:
Coxsackie virus; EV-71; Metal ion dependent phosphotransfer; Nucleotide transfer reaction; PCP-consensus sequence; Peptide priming; Poliovirus; RNA polymerase
- PMID:
- 26074065
- [PubMed - as supplied by publisher]
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