Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase.
AUTOR(ES)
Mazumder, A
RESUMO
We report the activities of HIV integrase protein on a novel DNA substrate, consisting of a pair of gapped duplex molecules. Integrase catalyzed an intermolecular disintegration reaction that requires positioning of a pair of the gapped duplexes in a configuration that resembles the intgration intermediate. However, the major reaction resulted from an intramolecular reaction involving a single gapped duplex, giving rise to a hairpin. Surprisingly, a deletion mutant of integrase that lacks both the amino and carboxyl terminal regions still catalyzed the intermolecular disintegration reaction, but supported only a very low level of the intramolecular reaction. The central core region of integrase is therefore sufficient to both bind the gapped duplex DNA and juxtapose a pair of such molecules through protein-protein interactions. We suggest that the branched DNA structures of the previously reported disintegration substrate, and the intermolecular disintegration substrate described here, assist in stabilizing protein-protein interactions that otherwise require the amino and carboxy terminal regions of integrase.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=307927Documentos Relacionados
- A novel assay for the DNA strand-transfer reaction of HIV-1 integrase.
- A conditionally replicating HIV-1 vector interferes with wild-type HIV-1 replication and spread.
- Analysis of wild-type and mutant p21WAF-1 gene activities.
- Inhibitors of HIV-1 replication that inhibit HIV integrase.
- Wild-Type and Mutant Stocks of Mormoniella