Related Content
Search Google Scholar for:
|
|
Science 17 April 1987:
Vol. 236. no. 4799, pp. 305 - 308
DOI: 10.1126/science.2436298
|
|
Articles
Science, Vol 236, Issue 4799, 305-308
Copyright © 1987 by American Association for the Advancement of Science
Expression and processing of the AIDS virus reverse transcriptase in Escherichia coli
WG Farmerie,
DD Loeb,
NC Casavant,
CA Hutchison 3rd,
MH Edgell,
and
R Swanstrom
The ability to express the genes of pathogenic human viruses, such as the acquired immune deficiency syndrome (AIDS) virus (also called human immunodeficiency virus) in bacterial cells affords the opportunity to study proteins that are ordinarily difficult or inconvenient to obtain in amounts sufficient for detailed analysis. A segment of the AIDS virus pol gene was expressed in Escherichia coli. Expression resulted in the appearance of reverse transcriptase activity in the bacterial cell extracts. The extracts contained two virus-related polypeptides that have the same apparent molecular weights as the two processed forms of virion-derived reverse transcriptase (p66 and p51). The formation of these two polypeptides depended on the coexpression of sequences located near the 5' end of the pol gene, a region that is thought to encode a viral protease. This bacterial system appears to generate mature forms of the AIDS virus reverse transcriptase by a proteolytic pathway equivalent to that which occurs during virus infection of human cells.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- Reverse transcription of the HIV-1 pandemic.
- A. Basavapathruni and K. S. Anderson (2007)
FASEB J
21, 3795-3808
| Abstract »
| Full Text »
| PDF »
- HIV-1 preferentially binds receptors copatched with cell-surface elastase.
- C. L. Bristow, D. R. Mercatante, and R. Kole (2003)
Blood
102, 4479-4486
| Abstract »
| Full Text »
| PDF »
- Slow Human Immunodeficiency Virus (HIV) Infectivity Correlated with Low HIV Coreceptor Levels.
- C. L. Bristow (2001)
Clin. Vaccine Immunol.
8, 932-936
| Abstract »
| Full Text »
| PDF »
- Human T-Cell Leukemia Virus Type 1 Reverse Transcriptase (RT) Originates from the pro and pol Open Reading Frames and Requires the Presence of RT-RNase H (RH) and RT-RH-Integrase Proteins for Its Activity.
- B. Trentin, N. Rebeyrotte, and R. Z. Mamoun (1998)
J. Virol.
72, 6504-6510
| Abstract »
| Full Text »
| PDF »
- A genetic approach for identifying critical residues in the fingers and palm subdomains of HIV-1 reverse transcriptase.
- J. A. Wrobel, S.-F. Chao, M. J. Conrad, J. D. Merker, R. Swanstrom, G. J. Pielak, and C. A. Hutchison III (1998)
PNAS
95, 638-645
| Abstract »
| Full Text »
| PDF »
- Functionally interacting telomerase RNAs in the yeast telomerase complex.
- J. Prescott and E. H. Blackburn (1997)
Genes & Dev.
11, 2790-2800
| Abstract »
| Full Text »
| PDF »
- Sequence requirements of the HIV-1 protease flap region determined by saturation mutagenesis and kinetic analysis of flap mutants.
- W. Shao, L. Everitt, M. Manchester, D. D. Loeb, C. A. Hutchison III, and R. Swanstrom (1997)
PNAS
94, 2243-2248
| Abstract »
| Full Text »
| PDF »
- Conversion of Thymidylate Synthase into an HIV Protease Substrate.
- J.-J. Kupiec, S. Hazebrouck, T. Leste-Lasserre, and P. Sonigo (1996)
J. Biol. Chem.
271, 18465-18470
| Abstract »
| Full Text »
| PDF »
- Molecular modeling of the HIV-1 protease and its substrate binding site.
- I. Weber, M Miller, M Jaskolski, J Leis, A. Skalka, and A Wlodawer (1989)
Science
243, 928-931
| Abstract »
| PDF »
- Regulation of HIV and HTLV gene expression..
- H Varmus (1988)
Genes & Dev.
2, 1055-1062
| PDF »
- HIV-1 reverse transcriptase is a target for cytotoxic T lymphocytes in infected individuals.
- B. Walker, C Flexner, T. Paradis, T. Fuller, M. Hirsch, R. Schooley, and B Moss (1988)
Science
240, 64-66
| Abstract »
| PDF »
|
|
