Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G

Kuan Ming Chen, Natalia Martemyanova, Yongjian Lu, Keisuke Shindo, Hiroshi Matsuo, Reuben S. Harris

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31/69) alanine substitution derivatives of APOBEC3G198-384 retained significant to full levels of activity. These data corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core.

Original languageEnglish (US)
Pages (from-to)4761-4766
Number of pages6
JournalFEBS Letters
Volume581
Issue number24
DOIs
StatePublished - Oct 2 2007
Externally publishedYes

Keywords

  • APOBEC3G
  • DNA cytosine deamination
  • DNA editing
  • Hypermutation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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