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PMID: 2417240 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Andrews NC, Baltimore D

Abstract

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.

MeSH Terms
HeLa Cells/enzymology Humans Poliovirus/enzymology,growth & development RNA Nucleotidyltransferases/isolation & purification,metabolism RNA-Dependent RNA Polymerase/metabolism RNA-Directed DNA Polymerase/metabolism Templates, Genetic Virus Replication
Chemicals
RNA Nucleotidyltransferases UTP-RNA uridylyltransferase RNA-Dependent RNA Polymerase RNA-Directed DNA Polymerase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Andrews N C
Baltimore D
References (38)
38 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1986-01-00
Pages
221-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC322829
Subset
IM
Grants
NIGMS NIH HHS · T32 GM007753 · United States
NIGMS NIH HHS · 2T 32 GM07753-06 · United States
NIAID NIH HHS · AI22346 · United States
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