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Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G
Author(s) -
Chen Kuan-Ming,
Martemyanova Natalia,
Lu Yongjian,
Shindo Keisuke,
Matsuo Hiroshi,
Harris Reuben S.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.076
Subject(s) - apobec3g , cytosine deaminase , mutagenesis , chemistry , dna , retrotransposon , biochemistry , dna replication , biology , genetics , mutation , cytidine deaminase , mutant , gene , genetic enhancement , transposable element
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.