Nucleic Acids Research Advance Access originally published online on October 11, 2006
Nucleic Acids Research 2006 34(19):5683-5694; doi:10.1093/nar/gkl721
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Nucleic Acids Research, 2006, Vol. 34, No. 19 5683-5694
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Nucleic Acid Enzymes |
Evolutionarily conserved and non-conserved retrovirus restriction activities of artiodactyl APOBEC3F proteins
1 Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Minneapolis, MN 55455, USA 2 Institute for Molecular Virology Minneapolis, MN 55455, USA 3 Arnold and Mabel Beckman Center for Transposon Research Minneapolis, MN 55455, USA 4 University of Iceland, Institute for Experimental Pathology Keldur v/Vesturlandsveg, 112 Reykjavík, Iceland 5 Department of Animal Sciences, University of Minnesota St Paul, MN 55108, USA
*To whom correspondence should be addressed. Tel: +1 612 624 0457; Fax: +1 612 625 2163; Email: rsh{at}umn.edu
Received August 4, 2006. Revised September 16, 2006. Accepted September 18, 2006.
The APOBEC3 proteins are unique to mammals. Many inhibit retrovirus infection through a cDNA cytosine deamination mechanism. HIV-1 neutralizes this host defense through Vif, which triggers APOBEC3 ubiquitination and degradation. Here, we report an APOBEC3F-like, double deaminase domain protein from three artiodactyls: cattle, pigs and sheep. Like their human counterparts, APOBEC3F and APOBEC3G, the artiodactyl APOBEC3F proteins are DNA cytosine deaminases that locate predominantly to the cytosol and can inhibit the replication of HIV-1 and MLV. Retrovirus restriction is attributable to deaminase-dependent and -independent mechanisms, as deaminase-defective mutants retain significant anti-retroviral activity. However, unlike human APOBEC3F and APOBEC3G, the artiodactyl APOBEC3F proteins have an active N-terminal DNA cytosine deaminase domain, which elicits a broader dinucleotide deamination preference, and they are resistant to HIV-1 Vif. These data indicate that DNA cytosine deamination; sub-cellular localization and retrovirus restriction activities are conserved in mammals, whereas active site location, local mutational preferences and Vif susceptibility are not. Together, these studies indicate that some properties of the mammal-specific, APOBEC3-dependent retroelement restriction system are necessary and conserved, but others are simultaneously modular and highly adaptable.
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