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Journal of Virology, April 1999, p. 3176-3183, Vol. 73, No. 4
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Dissecting the Role of the N-Terminal Domain of Human Immunodeficiency Virus Integrase by trans-Complementation Analysis

Fusinita M. I. van den Ent, Arnold Vos, and Ronald H. A. Plasterk*

Division of Molecular Biology, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands

Received 4 September 1998/Accepted 18 January 1999

The human immunodeficiency virus (HIV) integrase protein (IN) catalyzes two reactions required to integrate HIV DNA into the human genome: 3' processing of the viral DNA ends and integration. IN has three domains, the N-terminal zinc-binding domain, the catalytic core, and the C-terminal SH3 domain. Previously, it was shown that IN proteins mutated in different domains could complement each other. We now report that this does not require any overlap between the two complementing proteins; an N-terminal domain, provided in trans, can restore IN activity of a mutant lacking this domain. Only the zinc-coordinating form of the N-terminal domain can efficiently restore IN activity of an N-terminal deletion mutant. This suggests that interaction between different domains of IN is needed for functional multimerization. We find that the N-terminal domain of feline immunodeficiency virus IN can support IN activity of an N-terminal deletion mutant of HIV type 2 IN. These cross-complementation experiments indicate that the N-terminal domain contributes to the recognition of specific viral DNA ends.

* Corresponding author. Mailing address: Division of Molecular Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands. Phone: 31-20-5122081. Fax: 31-20-5122086. E-mail: rplas{at}nki.nl.

Journal of Virology, April 1999, p. 3176-3183, Vol. 73, No. 4
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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