Restriction of HIV-1 by APOBEC3G is cytidine deaminase-dependent

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Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G

APOBEC3G (A3G), a host protein that inhibits HIV-1 reverse transcription and replication in the absence of Vif, displays cytidine deaminase and single-stranded (ss) nucleic acid binding activities. HIV-1 nucleocapsid protein (NC) also binds nucleic acids and has a unique property, nucleic acid chaperone activity, which is crucial for efficient reverse transcription. Here we report the interplay...

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LYMPHOID NEOPLASIA APOBEC3G enhances lymphoma cell radioresistance by promoting cytidine deaminase-dependent DNA repair

1Department of Pathology and the Lautenberg Center for General and Tumor Immunology, Hebrew University–Hadassah Medical School, Jerusalem, Israel; 2Institute of Chemistry and Center for Nanoscience and Nanotechnology, Hebrew University, Jerusalem, Israel; 3Department of Genetics, Institute of Life Sciences, Hebrew University, Jerusalem, Israel; 4Division of Hematology and Bone Marrow Transplant...

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APOBEC3G enhances lymphoma cell radioresistance by promoting cytidine deaminase-dependent DNA repair.

APOBEC3 proteins catalyze deamination of cytidines in single-stranded DNA (ssDNA), providing innate protection against retroviral replication by inducing deleterious dC > dU hypermutation of replication intermediates. APOBEC3G expression is induced in mitogen-activated lymphocytes; however, no physiologic role related to lymphoid cell proliferation has yet to be determined. Moreover, whether AP...

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RNA-Dependent Oligomerization of APOBEC3G Is Required for Restriction of HIV-1

The human cytidine deaminase APOBEC3G (A3G) is a potent inhibitor of retroviruses and transposable elements and is able to deaminate cytidines to uridines in single-stranded DNA replication intermediates. A3G contains two canonical cytidine deaminase domains (CDAs), of which only the C-terminal one is known to mediate cytidine deamination. By exploiting the crystal structure of the related tetr...

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The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme

APOBEC3G is a cytidine deaminase with two homologous domains and restricts retroelements and HIV-1. APOBEC3G deaminates single-stranded DNAs via its C-terminal domain, whereas the N-terminal domain is considered non-catalytic. Although APOBEC3G is known to bind RNAs, APOBEC3G-mediated RNA editing has not been observed. We recently discovered RNA editing by the single-domain enzyme APOBEC3A in i...

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ژورنال

عنوان ژورنال: Virology

سال: 2009

ISSN: 0042-6822

DOI: 10.1016/j.virol.2009.02.026