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J. Biol. Chem., Vol. 277, Issue 30, 27489-27493, July 26, 2002
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From the Aaron Diamond AIDS Research Center, The Rockefeller
University, New York, New York 10016
We have previously shown that human
immunodeficiency virus-1 (HIV-1) integrase is an unstable
protein and a substrate for the N-end rule degradation pathway.
This degradation pathway shares its ubiquitin-conjugating enzyme, Rad6,
with the post-replication/translesion DNA repair pathway. Because DNA
repair is thought to play an essential role in HIV-1 integration, we
investigated whether other molecules of this DNA repair pathway could
interact with integrase. We observed that co-expression of human Rad18
induced the accumulation of an otherwise unstable form of HIV-1
integrase. This accumulation occurred even though hRAD18 possesses a
RING finger domain, a structure that is generally associated with E3
ubiquitin ligase function and protein degradation. Evidence for an
interaction between integrase and hRad18 was obtained through
reciprocal co-immunoprecipitation. Moreover we found that a
162-residue region of hRad18 (amino acids 65-226) was sufficient for
both integrase stabilization and interaction. Finally, we observed that
HIV-1 integrase co-localized with hRad18 in nuclear structures in a
subpopulation of co-transfected cells. Taken together, these findings
identify hRad18 as a novel interacting partner of HIV-1 integrase and
suggest a role for post-replication/translesion DNA repair in the
retroviral integration process.
Interaction of HIV-1 Integrase with DNA Repair Protein
hRad18*
, and
*
This work was supported in part by Columbia-Rockefeller
Center for AIDS Research Grant P30 AI 42848 (to L. C. F. M.) from the NIAID, National Institutes of Health, by internal funding from the
Aaron Diamond AIDS Research Center, and National Institutes of Health
Grant 1R01 AI47054-01 (to M. A. M).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Institut Pasteur, Unite d'Immunologie Virale, 28 rue du Dr Roux, 75724 Paris Cedex 15, France.
§
To whom correspondence should be addressed. Tel.: 212-448-5060;
Fax: 212-448-5159; E-mail: mmuesing@adarc.org.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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