Uracil DNA glycosylase initiates degradation of HIV-1 cDNA containing misincorporated dUTP and prevents viral integration
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- Amy F. Weil
- Departments of aPharmacology and Molecular Sciences and
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- Devlina Ghosh
- Departments of aPharmacology and Molecular Sciences and
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- Yan Zhou
- Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205;
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- Lauren Seiple
- Departments of aPharmacology and Molecular Sciences and
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- Moira A. McMahon
- Ludwig Institute for Cancer Research and Department of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, CA 92093; and
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- Adam M. Spivak
- Department of Medicine, University of Utah School of Medicine, Salt Lake City, UT 84132
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- Robert F. Siliciano
- Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205;
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- James T. Stivers
- Departments of aPharmacology and Molecular Sciences and
書誌事項
- 公開日
- 2013-01-22
- DOI
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- 10.1073/pnas.1219702110
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:title>Significance</jats:title> <jats:p>Misincorporation of dUTP into DNA is detrimental to eukaryotes, prokaryotes, and viruses. This study reveals the fate of uracilated HIV-1 DNA in human cells. Early stages of the viral life cycle are unaffected, but integration of uracilated viral DNA into the host genome is prevented. This effect is wholly dependent on the presence of UNG2, a nuclear enzyme that excises uracil from DNA. This study establishes that UNG2 is a restriction factor for uracilated HIV-1 DNA and explains why this pathway is not fully engaged in CD4+ T cells and macrophages.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 110 (6), E448-, 2013-01-22
Proceedings of the National Academy of Sciences