A Caltech Library Service

Human immunodeficiency virus tat-activated expression of poliovirus protein 2A inhibits mRNA translation

Sun, Xiao-Hong and Baltimore, David (1989) Human immunodeficiency virus tat-activated expression of poliovirus protein 2A inhibits mRNA translation. Proceedings of the National Academy of Sciences of the United States of America, 86 (7). pp. 2143-2146. ISSN 0027-8424. doi:10.1073/pnas.86.7.2143.

PDF - Published Version
See Usage Policy.


Use this Persistent URL to link to this item:


To study the effect of poliovirus protein 2A on cellular RNA translation, the tat control system of human immunodeficiency virus (HIV) was used. Protein 2A was expressed from a plasmid construct (pHIV/2A) incorporating the HIV long terminal repeat. Protein synthesis was measured by using chloramphenicol acetyltransferase as a reporter gene driven by the Rous sarcoma virus long terminal repeat. When HIV/2A was contransfected with the reporter, addition of a tat-producing plasmid caused at least a 50-fold drop in chloramphenicol acetyltransferase synthesis. A HeLa cell line carrying HIV/2A was established. In it, tat expression caused more than a 10-fold drop in chloramphenicol acetyltransferase synthesis from the reporter plasmid. Furthermore, 2A induction by tat caused cleavage of the cellular translation factor P220, a part of eukaryotic translation initiation factor 4F. Thus protein 2A can, by itself, carry out the inhibition of cellular protein synthesis characteristic of a poliovirus infection. Also, the HIV tat activation provides a very effective method to control gene expression in mammalian cells.

Item Type:Article
Related URLs:
URLURL TypeDescription CentralArticle
Baltimore, David0000-0001-8723-8190
Additional Information:© 1989 by the National Academy of Sciences. Contributed by David Baltimore, December 19, 1988. We thank Jing-po Li, Didier Trono, and Raul Andino for suggestions, Nahum Sonenberg for the anti-P220 serum, and Sunyoung Kim for the HIV/CAT plasmid. This work was supported by grants from the National Institute of Allergy and Infectious Diseases and the National Institute of General Medical Sciences. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Funding AgencyGrant Number
National Institute of Allergy and Infectious DiseasesUNSPECIFIED
National Institute of General Medical SciencesUNSPECIFIED
Subject Keywords:trans-activation; protein synthesis; protease
Issue or Number:7
Record Number:CaltechAUTHORS:SUNpnas89
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:7714
Deposited By: Tony Diaz
Deposited On:17 Jul 2007
Last Modified:08 Nov 2021 20:45

Repository Staff Only: item control page