a comparison of two single-stranded dna binding models by mutational analysis of apobec3g比较两个单链dna结合模型apobec3g的突变分析.pdfVIP
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a comparison of two single-stranded dna binding models by mutational analysis of apobec3g比较两个单链dna结合模型apobec3g的突变分析
Biology 2012, 1, 260-276; doi:10.3390/biology1020260
OPEN ACCESS
biology
ISSN 2079-7737
/journal/biology
Article
A Comparison of Two Single-Stranded DNA Binding Models by
Mutational Analysis of APOBEC3G
Keisuke Shindo †, Ming Li, Phillip J. Gross, William L. Brown, Elena Harjes, Yongjian Lu,
Hiroshi Matsuo * and Reuben S. Harris *
Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology,
University of Minnesota, Minneapolis, MN 55455, USA;
E-Mails: shind009@kuhp.kyoto-u.ac.jp (K.S.); mingli@ (M.L.); gros0287@ (P.J.G.);
brown344@ (W.L.B.); harje002@ (E.H.); luxxx079@ (Y.L.)
† Present address: Department of Hematology and Oncology, Graduate School of Medicine,
Kyoto University, Kyoto, Kyoto 606-8507, Japan.
* Authors to whom correspondence should be addressed; E-Mails: matsu029@ (H.M.);
rsh@ (R.S.H.); Tel.: +1-612-625-6100.
Received: 23 May 2012; in revised form: 1 July 2012 / Accepted: 14 July 2012 /
Published: 2 August 2012
Abstract: APOBEC3G is the best known of several DNA cytosine deaminases that
function to inhibit the replication of parasitic genetic elements including the lentivirus HIV.
Several high-resolution structures of the APOBEC3G catalytic domain have been
generated, but none reveal how this enzyme binds to substrate single-stranded DNA. Here,
we constructed a panel of APOBEC3G amino acid substitution mutants and performed a
series of biochemical, genetic, and structural assays to distinguish between “Brim” and
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