The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
A large nucleoprotein assembly at the ends of the viral DNA mediates retroviral DNA integration
Open accessAbstract
We have probed the nucleoprotein organization of Moloney murine leukemia virus (MLV) pre-integration complexes using a novel footprinting technique that utilizes a simplified in vitro phage Mu transposition system. We find that several hundred base pairs at each end of the viral DNA are organized in a large nucleoprotein complex, which we call the intasome. This structure is not formed when pre-integration complexes are made by infecting cells with integrase-minus virus, demonstrating a requirement for integrase. In contrast, footprinting of internal regions of the viral DNA did not reveal significant differences between pre-integration complexes with and without integrase. Treatment with high salt disrupts the intasome in parallel with loss of intermolecular integration activity. We show that a cellular factor is required for reconstitution of the intasome. Finally, we demonstrate that DNA-protein interactions involving extensive regions at the ends of the viral DNA are functionally important for retroviral DNA integration activity. Current in vitro integration systems utilizing purified integrase lack the full fidelity of the in vivo reaction. Our results indicate that both host factors and long viral DNA substrates may be required to reconstitute an in vitro system with all the hallmarks of DNA integration in vivo.
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“Furthermore, while the intasome structure covers only ~20 bp of vDNA, footprinting studies suggested that as much as 200–250 bp at each vDNA end are protected by a stable protein complex within retroviral PICs45,46.”
From Structure and function of retroviral integrase (2022) · cites this paper as [45]
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Cites
In Vivo Footprinting of a Muscle Specific Enhancer by Ligation Mediated PCR
Mueller, P. R., & Wold, B. J. (1989) · Science · doi:10.1126/science.2814500 · Cited by 928
Dyda, F., Hickman, A. B., Jenkins, T. M., Engelman, A., Craigie, R., & Davies, D. R. (1994) · Science · doi:10.1126/science.7801124 · Cited by 810 · cited 2×
“A triad of acidic residues that are critical for catalysis lies within the central core of integrase, and the crystal structure of this domain has been solved for both HIV-1 integrase (Dyda et al., 1994) and RSV integrase (Bujacz et al., 1995).”
BackgroundSelf-citationHIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer
Engelman, A., Mizuuchi, K., & Craigie, R. (1991) · Cell · doi:10.1016/0092-8674(91)90297-c · Cited by 655
Self-citationKatz, R. A., & Skalka, A. M. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.001025 · Cited by 524
Correct integration of retroviral DNA in vitro
Brown, P. O., Bowerman, B. A., VARMUS, H. E., & Bishop, J. M. (1987) · Cell · doi:10.1016/0092-8674(87)90287-x · Cited by 460
Craigie, R., Fujiwara, T., & Bushman, F. (1990) · Cell · doi:10.1016/0092-8674(90)90126-y · Cited by 409
Self-citationBrown, P. O., Bowerman, B., Varmus, H. E., & Bishop, J. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.8.2525 · Cited by 399
TRANSPOSITIONAL RECOMBINATION: Mechanistic Insights from Studies of Mu and Other Elements
Mizuuchi, K. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.005051 · Cited by 394
Self-citationRetroviral DNA integration: structure of an integration intermediate
Fujiwara, T., & Mizuuchi, K. (1988) · Cell · doi:10.1016/0092-8674(88)90071-2 · Cited by 385
Self-citationA nucleoprotein complex mediates the integration of retroviral DNA.Preprint
Bowerman, B. A., Brown, P. O., Bishop, J. M., & Varmus, H. E. (1989) · Genes & Development · doi:10.1101/gad.3.4.469 · Cited by 378
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Non-integrase mechanisms for dolutegravir resistance
Engelman, A. (2026) · Retrovirology · doi:10.1186/s12977-026-00678-5 · Cited by 1
Metadata
- Authors
- Wei, S., Mizuuchi, K., & Craigie, R.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Craigie, Robert
- Venue
- The EMBO Journal
- Published
- 1997-12-15
- Volume
- 16
- Issue
- 24
- Pages
- 7511-7520
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1170350
- OpenAlex
- W2022750544
- Cited by
- 102
- References
- 47
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 1 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 3 · 2018: 3 · 2017: 2 · 2016: 1 · 2015: 5 · 2014: 4 · 2013: 3 · 2012: 2
- FWCI
- 2.24
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Keywords
- retroviral integration, intasome, Moloney murine leukemia virus, preintegration complex, integrase, nucleoprotein complexes, protein-DNA interactions, host factors
- MeSH terms
- Animals, Base Composition, Base Sequence, DNA, DNA Transposable Elements, DNA-Binding Proteins, DNA, Viral, Molecular Sequence Data, Moloney murine leukemia virus, Nucleoproteins, Oligodeoxyribonucleotides, Bacteriophage mu, Polymerase Chain Reaction, Mutagenesis, Insertional, Virus Integration, DNA Footprinting, Mice
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