ArticleThe Journal of biological chemistry2012
Single-stranded DNA scanning and deamination by APOBEC3G cytidine deaminase at single molecule resolution.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- RNase E searches for cleavage sites in RNA by linear diffusion: direct evidence from single-molecule FRET.Nucleic acids research · 2024Article
- Article
- Article
- Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G.Nature communications · 2020Article
- Article
- Single molecule kinetics uncover roles for E. coli RecQ DNA helicase domains and interaction with SSB.Nucleic acids research · 2018Article
- Computational Model and Dynamics of Monomeric Full-Length APOBEC3G.ACS central science · 2017Article
- Enzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B.Nucleic acids research · 2017Article
- Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G.Nature communications · 2017Article
- Review
- Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Nucleic acids research · 2017Article
- Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.Journal of virology · 2017Article
- Dynamic unwrapping of nucleosomes by HsRAD51 that includes sliding and rotational motion of histone octamers.Nucleic acids research · 2017Article
- APOBEC3 proteins can copackage and comutate HIV-1 genomes.Nucleic acids research · 2016Article
- Inhibition of APOBEC3G activity impedes double-stranded DNA repair.The FEBS journal · 2016Article
- Activation-induced deoxycytidine deaminase (AID) co-transcriptional scanning at single-molecule resolution.Nature communications · 2015Article
- Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.The Journal of biological chemistry · 2015Article
- APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.Scientific reports · 2015Article
- Random-walk enzymes.Physical review. E, Statistical, nonlinear, and soft matter physics · 2015Article
- Single-Molecule Pull-Down FRET to Dissect the Mechanisms of Biomolecular Machines.Methods in enzymology · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
APOBEC3G (Apo3G) is a single-stranded (ss)DNA cytosine deaminase that eliminates HIV-1 infectivity by converting C → U in numerous small target motifs on the minus viral cDNA. Apo3G deaminates linear ssDNA in vitro with pronounced spatial asymmetry favoring the 3' → 5' direction. A similar polarity observed in vivo is believed responsible for initiating localized C → T mutational gradients that inactivate the virus. When compared with double-stranded (ds)DNA scanning enzymes, e.g. DNA glycosylases that excise rare aberrant bases, there is a paucity of mechanistic studies on ssDNA scanning enzymes. Here, we investigate ssDNA scanning and motif-targeting mechanisms for Apo3G using single molecule Förster resonance energy transfer. We address the specific issue of deamination asymmetry within the general context of ssDNA scanning mechanisms and show that Apo3G scanning trajectories, ssDNA contraction, and deamination efficiencies depend on motif sequence, location, and ionic strength. Notably, we observe the presence of bidirectional quasi-localized scanning of Apo3G occurring proximal to a 5' hot motif, a motif-dependent DNA contraction greatest for 5' hot > 3' hot > 5' cold motifs, and diminished mobility at low salt. We discuss the single molecule Förster resonance energy transfer data in terms of a model in which deamination polarity occurs as a consequence of Apo3G binding to ssDNA in two orientations, one that is catalytically favorable, with the other disfavorable.
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