Purification of a terminal uridylyltransferase that acts as host factor in the in vitro poliovirus replicase reaction.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Andrews, NC; Baltimore, D

Published Date

  • January 1, 1986

Published In

Volume / Issue

  • 83 / 2

Start / End Page

  • 221 - 225

PubMed ID

  • 2417240

Pubmed Central ID

  • PMC322829

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.83.2.221


  • eng

Conference Location

  • United States