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© Charles DAUGUET, Institut Pasteur
HIV particles
Publication : The Journal of biological chemistry

Interaction of HIV-1 integrase with DNA repair protein hRad18

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 16 May 2002

Mulder LC, Chakrabarti LA, Muesing MA

Link to Pubmed [PMID] – 12016221

J. Biol. Chem. 2002 Jul;277(30):27489-93

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.

http://www.ncbi.nlm.nih.gov/pubmed/12016221