ATP is required for initiation of poliovirus RNA synthesis in vitro: demonstration of tyrosine-phosphate linkage between in vitro-synthesized RNA and genome-linked protein.
AUTOR(ES)
Morrow, C D
RESUMO
Poliovirus replicase- and host factor-catalyzed copying of 3'-terminal polyadenylic acid [poly(A)] of poliovirion RNA was studied. Host factor-stimulated synthesis of polyuridylic acid [poly(U)] by the replicase required ATP in addition to UTP. ATP was not required for the oligouridylic acid-primed copying of 3'-terminal poly(A) of virion RNA. GTP, CTP, and AMP-PCP (5'-adenylyl beta-gamma methylenediphosphate, an ATP analog) could not replace ATP in host factor-stimulated synthesis of poly(U). Antibodies to poliovirus genome-linked protein (VPg) specifically precipitated in vitro-synthesized poly(U) from a host factor-stimulated reaction. The poly(U) synthesized in a host factor-stimulated reaction was shown to be attached to VPg precursor polypeptide(s) via a tyrosine-phosphate bond as found in poliovirion VPg-RNA.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=255660Documentos Relacionados
- O4-(5'-uridylyl)tyrosine is the bond between the genome-linked protein and the RNA of poliovirus.
- In vitro-synthesized hepatitis delta virus RNA initiates genome replication in cultured cells.
- Three-dimensional model of the potyviral genome-linked protein.
- Mutational analysis of the genome-linked protein VPg of poliovirus.
- Membrane-dependent uridylylation of the genome-linked protein VPg of poliovirus.
