Factors required for the Uridylylation of the foot-and-mouth disease virus 3B1, 3B2, and 3B3 peptides by the RNA-dependent RNA polymerase (3Dpol) in vitro.
The 5' terminus of picornavirus genomic RNA is covalently linked to the virus-encoded peptide 3B (VPg). Foot-and-mouth disease virus (FMDV) is unique in encoding and using 3 distinct forms of this peptide. These peptides each act as primers for RNA synthesis by the virus-encoded RNA polymerase 3D(pol). To act as the primer for positive-strand RNA synthesis, the 3B peptides have to be uridylylated to form VPgpU(pU). For certain picornaviruses, it has been shown that this reaction is achieved by the 3D(pol) in the presence of the 3CD precursor plus an internal RNA sequence termed a cis-acting replication element (cre). The FMDV cre has been identified previously to be within the 5' untranslated region, whereas all other picornavirus cre structures are within the viral coding region. The requirements for the in vitro uridylylation of each of the FMDV 3B peptides has now been determined, and the role of the FMDV cre (also known as the 3B-uridylylation site, or bus) in this reaction has been analyzed. The poly(A) tail does not act as a significant template for FMDV 3B uridylylation.
Nayak
Arabinda
A
BBSRC Institute for Animal Health, Pirbright, Woking, Surrey GU24 ONF, United Kingdom.
Goodfellow
Ian G
IG
Belsham
Graham J
GJ
D004742:Enhancer Elements, Genetic; D029544:Foot-and-Mouth Disease Virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D012324:RNA-Dependent RNA Polymerase / Q000378:metabolism*; D014542:Uridine Monophosphate / Q000378:metabolism*; D014758:Viral Core Proteins / Q000378:metabolism*; D014779:Virus Replication
D010455:Peptides; D012367:RNA, Viral; D014758:Viral Core Proteins; D014542:Uridine Monophosphate; D012324:RNA-Dependent RNA Polymerase