Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence in vitro
Identifieur interne : 000820 ( Istex/Curation ); précédent : 000819; suivant : 000821Moloney murine leukemia virus in protein from disrupted virions binds and specifically cleaves its target sequence in vitro
Auteurs : Lance K. Ishimoto [États-Unis] ; Mike Halperin [États-Unis] ; Champouxi James J. [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1991.
English descriptors
- Teeft :
- Academic press, Assay, Avian myeloblastosis virus, Bind oligonucleotides, Binding activity, Binding assay, Binding reaction, Binding reactions, Champoux, Cleavage, Cleavage activity, Cleavage events, Cleavage product, Control oligonucleotide, Correct integration, Craigie, Dldc, Duplex, Duplex form, Duplex oligonucleotides, Endonuclease, Endonuclease activity, Extensive analysis, Fujiwara, Fusion product, Goff, Integration machinery, Integration reaction, Inverted, Major endonuclease activity, Moloney, Moloney murine leukemia virus, Murine, Nucleotide sequence, Oligonucleotide, Oligonucleotide substrates, Oligonucleotides, Path3 vector, Poly dldc, Polynucleotide kinase, Preimmune serum, Present evidence, Previous studies, Processing reaction, Processing step, Retarded mobility, Retroviral, Retroviral integration, Shift patterns, Sizing ladder, Specific binding, Specific cleavage, Such cleavage, Terminal sequences, Terminus, Unbound oligonucleotide, Unlabeled, Unlabeled lane, Varmus, Viral, Virion.
Abstract
Abstract: The integration of retroviral DNA plays an essential role in the viral life cycle. Previous studies of the Moloney murine leukemia virus (M-MuLV) have shown that viral integration is mediated by the integrase (IN) protein acting on the 13-bp inverted repeats that flank the linear viral DNA produced during reverse transcription. Prior studies have also shown that when the M-MuLV IN protein is produced in Escherichia coli it retains an ability to specifically associate with the viral inverted repeats (Krogstad and Champoux, 1990). In this study we present evidence that the IN protein present in detergent-disrupted virions is capable of specifically interacting with double-stranded oligonucleotides that correspond to the viral inverted repeats, and that this interaction may change after integration-related processing of the viral att sites. We further present evidence that, in vitro, detergent-disrupted virions are capable of specifically cleaving ds-IR oligonucleotides in an IN-dependent reaction that mimics the trimming step that precedes integration.
Url:
DOI: 10.1016/0042-6822(91)90066-K
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<front><div type="abstract" xml:lang="en">Abstract: The integration of retroviral DNA plays an essential role in the viral life cycle. Previous studies of the Moloney murine leukemia virus (M-MuLV) have shown that viral integration is mediated by the integrase (IN) protein acting on the 13-bp inverted repeats that flank the linear viral DNA produced during reverse transcription. Prior studies have also shown that when the M-MuLV IN protein is produced in Escherichia coli it retains an ability to specifically associate with the viral inverted repeats (Krogstad and Champoux, 1990). In this study we present evidence that the IN protein present in detergent-disrupted virions is capable of specifically interacting with double-stranded oligonucleotides that correspond to the viral inverted repeats, and that this interaction may change after integration-related processing of the viral att sites. We further present evidence that, in vitro, detergent-disrupted virions are capable of specifically cleaving ds-IR oligonucleotides in an IN-dependent reaction that mimics the trimming step that precedes integration.</div>
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