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

FEBS Lett. 2007 Oct 2;581(24):4761-6. doi: 10.1016/j.febslet.2007.08.076. Epub 2007 Sep 7.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • APOBEC-3G Deaminase
  • Amino Acid Motifs
  • Chromatography, Gel
  • Cytidine Deaminase / chemistry*
  • Cytidine Deaminase / genetics
  • Cytidine Deaminase / metabolism*
  • DNA / metabolism*
  • Deamination
  • Gene Expression
  • Humans
  • Models, Molecular
  • Mutagenesis
  • Phenotype
  • Protein Structure, Tertiary
  • Structural Homology, Protein

Substances

  • DNA
  • APOBEC-3G Deaminase
  • APOBEC3G protein, human
  • Cytidine Deaminase