Dissecting the role of the N-terminal domain of human immunodeficiency virus integrase by trans-complementation analysis.

Abstract:

: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.

journal_name

J Virol

journal_title

Journal of virology

authors

van den Ent FM,Vos A,Plasterk RH

doi

10.1128/JVI.73.4.3176-3183.1999

subject

Has Abstract

pub_date

1999-04-01 00:00:00

pages

3176-83

issue

4

eissn

0022-538X

issn

1098-5514

journal_volume

73

pub_type

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