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Science 7 February 1992:
Vol. 255. no. 5045, pp. 723 - 726
DOI: 10.1126/science.1738845
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Articles

Science, Vol 255, Issue 5045, 723-726
Copyright © 1992 by American Association for the Advancement of Science

articles

Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus

SA Chow, KA Vincent, V Ellison, and PO Brown

Department of Pediatrics, Stanford University Medical Center, CA 94305.

In retroviral integration, the viral integration protein (integrase) mediates a concerted DNA cleavage-ligation reaction in which the target DNA is cleaved and the resulting 5' ends of target DNA are joined to the 3' ends of viral DNA. Through an oligonucleotide substrate that mimics the recombination intermediate formed by this initial cleavage-ligation reaction, the purified integrase of human immunodeficiency virus was shown to promote the same reaction in reverse, a process called disintegration. Analysis of a set of structurally related substrates showed that integrase could promote a range of DNA cleavage-ligation reactions. When the viral DNA component of the disintegration substrate was single-stranded, integrase could mediate a DNA splicing reaction analogous to RNA splicing.


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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
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Rejoining of DNA by the RAG1 and RAG2 Proteins.
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Implication of a Central Cysteine Residue and the HHCC Domain of Moloney Murine Leukemia Virus Integrase Protein in Functional Multimerization.
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J. Virol. 72, 1691-1698
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Dicaffeoylquinic and Dicaffeoyltartaric Acids Are Selective Inhibitors of Human Immunodeficiency Virus Type 1 Integrase.
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Antimicrob. Agents Chemother. 42, 140-146
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Potent Inhibitors of Human Immunodeficiency Virus Type 1 Integrase: Identification of a Novel Four-Point Pharmacophore and Tetracyclines as Novel Inhibitors.
N. Neamati, H. Hong, S. Sunder, G. W. A. Milne, and Y. Pommier (1997)
Mol. Pharmacol. 52, 1041-1055
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Mol. Pharmacol. 52, 771-780
   Abstract »    Full Text »
The Core Domain of HIV-1 Integrase Recognizes Key Features of Its DNA Substrates.
J. L. Gerton and P. O. Brown (1997)
J. Biol. Chem. 272, 25809-25815
   Abstract »    Full Text »    PDF »
Probing Interactions between Viral DNA and Human Immunodeficiency Virus Type 1 Integrase Using Dinucleotides.
A. Mazumder, H. Uchida, N. Neamati, S. Sunder, M. Jaworska-Maslanka, E. Wickstrom, F. Zeng, R. A. Jones, R. F. Mandes, H. K. Chenault, et al. (1997)
Mol. Pharmacol. 51, 567-575
   Abstract »    Full Text »
Central Core Domain of Retroviral Integrase Is Responsible for Target Site Selection.
Y. Shibagaki and S. A. Chow (1997)
J. Biol. Chem. 272, 8361-8369
   Abstract »    Full Text »    PDF »
Disruption of the terminal base pairs of retroviral DNA during integration..
B P Scottoline, S Chow, V Ellison, and P O Brown (1997)
Genes & Dev. 11, 371-382
   Abstract »    PDF »
Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity.
R. Zheng, T. M. Jenkins, and R. Craigie (1996)
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Retroviral Integrase, Putting the Pieces Together.
M. D. Andrake and A. M. Skalka (1996)
J. Biol. Chem. 271, 19633-19636
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A Soluble Active Mutant of HIV-1 Integrase.
T. M. Jenkins, A. Engelman, R. Ghirlando, and R. Craigie (1996)
J. Biol. Chem. 271, 7712-7718
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The Metal Ion-induced Cooperative Binding of HIV-1 Integrase to DNA Exhibits a Marked Preference for Mn(II) Rather than Mg(II).
I. K. Pemberton, M. Buckle, and H. Buc (1996)
J. Biol. Chem. 271, 1498-1506
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Multimerization Determinants Reside in Both the Catalytic Core and C Terminus of Avian Sarcoma Virus Integrase.
M. D. Andrake and A. M. Skalka (1995)
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Characterization of the Human Spuma Retrovirus Integrase by Site-directed Mutagenesis, by Complementation Analysis, and by Swapping the Zinc Finger Domain of HIV-1.
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An Essential Interaction between Distinct Domains of HIV-1 Integrase Mediates Assembly of the Active Multimer.
V. Ellison, J. Gerton, K. A. Vincent, and P. O. Brown (1995)
J. Biol. Chem. 270, 3320-3326
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Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases.
F Dyda, A. Hickman, T. Jenkins, A Engelman, R Craigie, and D. Davies (1994)
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Therapy for Human Immunodeficiency Virus Infection.
M. S. Hirsch and R. T. D'Aquila (1993)
N. Engl. J. Med. 328, 1686-1695
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Retroviral Integration Machinery as a Probe for DNA Structure and Associated Proteins.
H.-P. Muller, P.M. Pryciak, and H.E. Varmus (1993)
Cold Spring Harb Symp Quant Biol 58, 533-541
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An Inhibitory Monoclonal Antibody Binds at the Turn of the Helix-Turn-Helix Motif in the N-terminal Domain of HIV-1 Integrase.
J. Yi, J. W. Arthur, R. L. Dunbrack Jr., and A. M. Skalka (2000)
J. Biol. Chem. 275, 38739-38748
   Abstract »    Full Text »    PDF »
Nucleophile Selection for the Endonuclease Activities of Human, Ovine, and Avian Retroviral Integrases.
L. M. Skinner, M. Sudol, A. L. Harper, and M. Katzman (2001)
J. Biol. Chem. 276, 114-124
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Interactions of the Human T-cell Leukemia Virus Type-II Integrase with the Conserved CA in the Retroviral Long Terminal Repeat End.
T. Wang, A. J. Piefer, and C. B. Jonsson (2001)
J. Biol. Chem. 276, 14710-14717
   Abstract »    Full Text »    PDF »
Effect of HIV integrase inhibitors on the RAG1/2 recombinase.
M. Melek, J. M. Jones, M. H. O'Dea, G. Pais, T. R. Burke Jr., Y. Pommier, N. Neamati, and M. Gellert (2002)
PNAS 99, 134-137
   Abstract »    Full Text »    PDF »
HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase.
A. S. Espeseth, P. Felock, A. Wolfe, M. Witmer, J. Grobler, N. Anthony, M. Egbertson, J. Y. Melamed, S. Young, T. Hamill, et al. (2000)
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   Abstract »    Full Text »    PDF »


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