Key result
Terminal uridylyltransferase purified from HeLa cells acts as a host factor for poliovirus RNA polymerase by adding uridine residues to the 3' poly(A) end of virion RNA to form a hairpin primer.
The study demonstrates that the host factor required for in vitro poliovirus RNA synthesis is a terminal uridylyltransferase that creates a hairpin primer for the viral polymerase.
Identifies a host factor for poliovirus replication in vitro; leaves open relevance to cellular infection or antiviral strategies.
Poliovirus RNA polymerase requires a host factor to initiate RNA synthesis in vitro. The host factor was previously purified to near homogeneity from HeLa cells but was not assigned an enzymatic activity. This report describes the purification of a terminal uridylyltransferase that can act as host factor. By all criteria examined it is identical to the factor purified previously. It has the same molecular weight (68,000), chromatographic properties, and cellular localization. We present evidence that terminal uridylyltransferase can add uridine residues to the 3' poly(A) end of virion RNA and that these anneal back to the poly(A) and form a hairpin primer for polymerase.
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Andrews et al. (1986) studied Poliovirus replication (in vitro). Terminal uridylyltransferase (TUTase) was evaluated on TUTase activity and host factor activity in vitro. Terminal uridylyltransferase purified from HeLa cells acts as a host factor for poliovirus RNA polymerase by adding uridine residues to the 3' poly(A) end of virion RNA to form a hairpin primer.
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