Skip Navigation

This Article
Right arrow Print PDF (1607K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (45)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Mizrahi, V.
Right arrow Articles by Dudding, L. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mizrahi, V.
Right arrow Articles by Dudding, L. R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1990, Vol. 18, No. 18 5359-5363
© 1990

ENZYMOLOGY

Site-directed mutagenesis of the conserved Asp-443 and Asp-498 carboxy-terminal residues of HIV-1 reverse transcriptase

Valerie Mizrahi*, Martine T. Usdin, Alexis Harington and Lindsay R. Dudding

Molecular Biology Laboratory, School of Pathology of the South African Institute for Medical Research and University of the Witwatersrand PO Box 1038, Johannesburg 2000, South Africa

*To whom correspondence should be addressed

Received July 26, 1990. Accepted August 16, 1990.

Substitution of the conserved Asp-443 residue of HIV-1 reverse transcriptase by asparagine specifically suppressed the ribonuclease H activity of the enzyme without affecting the reverse transcriptase activity, suggesting involvement of this ionizable residue at the ribonuclease H active site. An analogous asparagine substitution of the Asp-498 residue yielded an unstable enzyme that was difficult to enzymatically characterize. However, the instability caused by the Asn-498 mutation was relieved by the introduction of a second distal Asn-443 substitution, yielding an enzyme with wild type reverse transcriptase activity, but lacking ribonuclease H activity.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Virol.Home page
M. E. Abram and M. A. Parniak
Virion Instability of Human Immunodeficiency Virus Type 1 Reverse Transcriptase (RT) Mutated in the Protease Cleavage Site between RT p51 and the RT RNase H Domain
J. Virol., September 15, 2005; 79(18): 11952 - 11961.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Wisniewski, Y. Chen, M. Balakrishnan, C. Palaniappan, B. P. Roques, P. J. Fay, and R. A. Bambara
Substrate Requirements for Secondary Cleavage by HIV-1 Reverse Transcriptase RNase H
J. Biol. Chem., August 2, 2002; 277(32): 28400 - 28410.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
J. G. Julias, A. L. Ferris, P. L. Boyer, and S. H. Hughes
Replication of Phenotypically Mixed Human Immunodeficiency Virus Type 1 Virions Containing Catalytically Active and Catalytically Inactive Reverse Transcriptase
J. Virol., July 15, 2001; 75(14): 6537 - 6546.
[Abstract] [Full Text]

Home page
 J. Virol.Home page
S. Werner and B. M. Wöhrl
Asymmetric Subunit Organization of Heterodimeric Rous Sarcoma Virus Reverse Transcriptase alpha beta : Localization of the Polymerase and RNase H Active Sites in the alpha Subunit
J. Virol., April 1, 2000; 74(7): 3245 - 3252.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
X. Zhan and R. J. Crouch
The Isolated RNase H Domain of Murine Leukemia Virus Reverse Transcriptase. RETENTION OF ACTIVITY WITH CONCOMITANT LOSS OF SPECIFICITY
J. Biol. Chem., August 29, 1997; 272(35): 22023 - 22029.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
J. Peliska and S. Benkovic
Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase
Science, November 13, 1992; 258(5085): 1112 - 1118.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
K. Komori, S. Sakae, H. Daiyasu, H. Toh, K. Morikawa, H. Shinagawa, and Y. Ishino
Mutational Analysis of the Pyrococcus furiosus Holliday Junction Resolvase Hjc Revealed Functionally Important Residues for Dimer Formation, Junction DNA Binding, and Cleavage Activities
J. Biol. Chem., December 15, 2000; 275(51): 40385 - 40391.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.