CaltechAUTHORS
  A Caltech Library Service

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

Andrews, Nancy C. and Baltimore, David (1986) Purification of a terminal uridylyltransferase that acts as host factor in the in vitro poliovirus replicase reaction. Proceedings of the National Academy of Sciences of the United States of America, 83 (2). pp. 221-225. ISSN 0027-8424. PMCID PMC322829. doi:10.1073/pnas.83.2.221. https://resolver.caltech.edu/CaltechAUTHORS:20120626-124326427

[img]
Preview
PDF - Published Version
See Usage Policy.

5MB

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20120626-124326427

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.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1073/pnas.83.2.221DOIArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/pmc322829/PubMed CentralArticle
ORCID:
AuthorORCID
Baltimore, David0000-0001-8723-8190
Additional Information:© 1986 National Academy of Sciences. Contributed by David Baltimore, September 3, 1985. We thank Daniel Levin for his gift of step 6 eiF2 and double-stranded RNA-dependent protein kinase. Margaret Baron synthesized the VPg peptide used in one experiment. The Massachusetts Institute of Technology Cell Culture Center cultured HeLa cells for purification. We thank Bernard Mathey-Prevot for his advice on protein purification. N.C.A. was partially supported by a Medical Scientist Training Program grant from the National Institute of General Medical Sciences (2T 32 GM07753-06); this work was also funded by a grant from the National Institute of Allergy and Infectious Diseases (AI22346).
Funders:
Funding AgencyGrant Number
NIH Predoctoral Fewllowship2T 32 GM07753-06
NIHAI22346
Subject Keywords:RNA synthesis; hairpin priming
Issue or Number:2
PubMed Central ID:PMC322829
DOI:10.1073/pnas.83.2.221
Record Number:CaltechAUTHORS:20120626-124326427
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20120626-124326427
Official Citation: N C Andrews and D Baltimore Purification of a terminal uridylyltransferase that acts as host factor in the in vitro poliovirus replicase reaction PNAS 1986 83 (2) 221-225
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:32099
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:26 Jun 2012 21:08
Last Modified:09 Nov 2021 21:15

Repository Staff Only: item control page