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The C-terminal cytidine deaminase domain of APOBEC3G itself undergoes intersegmental transfer for a target search, as revealed by real-time NMR monitoring

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Abstract

APOBEC3G (A3G), an anti-human immunodeficiency virus 1 factor, deaminates cytidines. We examined deamination of two cytidines located separately on substrate ssDNA by the C-terminal domain (CTD) of A3G using real-time NMR monitoring. The deamination preference between the two cytidines was lost when either the substrate or non-substrate ssDNA concentration increased. When the non-substrate ssDNA concentration increased, the deamination activity first increased, but then decreased. This indicates that even a single domain, A3G-CTD, undergoes intersegmental transfer for a target search.

Graphical abstract: The C-terminal cytidine deaminase domain of APOBEC3G itself undergoes intersegmental transfer for a target search, as revealed by real-time NMR monitoring

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Publication details

The article was received on 31 Jul 2017, accepted on 06 Sep 2017 and first published on 06 Sep 2017


Article type: Communication
DOI: 10.1039/C7CP05171A
Citation: Phys. Chem. Chem. Phys., 2018, Advance Article
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    The C-terminal cytidine deaminase domain of APOBEC3G itself undergoes intersegmental transfer for a target search, as revealed by real-time NMR monitoring

    K. Kamba, T. Nagata and M. Katahira, Phys. Chem. Chem. Phys., 2018, Advance Article , DOI: 10.1039/C7CP05171A

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