APOBEC-1 and AID are nucleo-cytoplasmic trafficking proteins but APOBEC3G cannot traffic

被引:27
作者
Bennett, Ryan P.
Diner, Elie
Sowden, Mark P.
Lees, Joshua A.
Wedekind, Joseph E.
Smith, Harold C.
机构
[1] Univ Rochester, Dept Biochem & Biophys, Rochester, NY 14642 USA
[2] Univ Rochester, James P Wilmot Ctr, Rochester, NY 14642 USA
关键词
APOBEC3G; AID; APOBEC-1; trafficking; NLS; NES;
D O I
10.1016/j.bbrc.2006.09.032
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Human APOBEC3G (hA3G) is a member of the APOBEC-1 related protein (ARP) family of cytidine deaminases. hA3G functions as a natural defense against endogenous retrotransposons and a multitude of retroviruses, most notably human immunodeficiency virus type I (HIV-1). Nothing is known about the cellular function of hA3G, however, upon HIV-1 infection hA3G functions as an antiviral factor by mutating viral single-stranded DNA during reverse transcription. Whereas homologous deaminases such as APOBEC-1 and AID act on RNA and DNA, respectively, in the cell nucleus, hA3G mutagenic activity appears to be restricted to the cytoplasm. We demonstrate that hA3G is not a nucleo-cytoplasmic shuttling protein like APOBEC-1 and AID, but is strongly retained in the cytoplasm through a mechanism that involves both the N and C-terminal regions of the protein. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:214 / 219
页数:6
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