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Nat Struct Mol Biol. 2006 May;13(5):392-9. Epub 2006 Apr 23.

APOBEC3G DNA deaminase acts processively 3' --> 5' on single-stranded DNA.

Author information

1
Department of Biological Sciences Molecular and Computational Section, University of Southern California, Los Angeles, California 90089-2910, USA.

Abstract

Akin to a 'Trojan horse,' APOBEC3G DNA deaminase is encapsulated by the HIV virion. APOBEC3G facilitates restriction of HIV-1 infection in T cells by deaminating cytosines in nascent minus-strand complementary DNA. Here, we investigate the biochemical basis for C --> U targeting. We observe that APOBEC3G binds randomly to single-stranded DNA, then jumps and slides processively to deaminate target motifs. When confronting partially double-stranded DNA, to which APOBEC3G cannot bind, sliding is lost but jumping is retained. APOBEC3G shows catalytic orientational specificity such that deamination occurs predominantly 3' --> 5' without requiring hydrolysis of a nucleotide cofactor. Our data suggest that the G --> A mutational gradient generated in viral genomic DNA in vivo could result from an intrinsic processive directional attack by APOBEC3G on single-stranded cDNA.

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PMID:
16622407
DOI:
10.1038/nsmb1086
[Indexed for MEDLINE]

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