title: Mice deficient in APOBEC2 and APOBEC3.
abstract: The activation-induced deaminase/apolipoprotein B-editing catalytic subunit 1 (AID/APOBEC) family comprises four groups of proteins. Both AID, a lymphoid-specific DNA deaminase that triggers antibody diversification, and APOBEC2 (function unknown) are found in all vertebrates examined. In contrast, APOBEC1, an RNA-editing enzyme in gastrointestinal cells, and APOBEC3 are restricted to mammals. The function of most APOBEC3s, of which there are seven in human but one in mouse, is unknown, although several human APOBEC3s act as host restriction factors that deaminate human immunodeficiency virus type 1 replication intermediates. A more primitive function of APOBEC3s in protecting against the transposition of endogenous retroelements has, however, been proposed. Here, we focus on mouse APOBEC2 (a muscle-specific protein for which we find no evidence of a deaminating activity on cytidine whether as a free nucleotide or in DNA) and mouse APOBEC3 (a DNA deaminase which we find widely expressed but most abundant in lymphoid tissue). Gene-targeting experiments reveal that both APOBEC2 (despite being an ancestral member of the family with no obvious redundancy in muscle) and APOBEC3 (despite its proposed role in restricting endogenous retrotransposition) are inessential for mouse development, survival, or fertility.
authors.affiliation: Medical Research Council Laboratory of Molecular Biology, Division of PNAC, Cambridge, UK.
authors.forename: Marie C
authors.initials: MC
authors.lastname: Mikl
authors.forename: Ian N
authors.initials: IN
authors.lastname: Watt
authors.forename: Mason
authors.initials: M
authors.lastname: Lu
authors.forename: Wolf
authors.initials: W
authors.lastname: Reik
authors.forename: Sarah L
authors.initials: SL
authors.lastname: Davies
authors.forename: Michael S
authors.initials: MS
authors.lastname: Neuberger
authors.forename: Cristina
authors.initials: C
authors.lastname: Rada
mesh_terms: D000071478:APOBEC Deaminases; D000071480:APOBEC-3G Deaminase; D000818:Animals; D015139:Blotting, Southern; D002470:Cell Survival; D003562:Cytidine / Q000378:metabolism; D003564:Cytidine Deaminase / Q000235:genetics* / Q000502:physiology*; D018076:DNA, Complementary / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D005298:Fertility; D005434:Flow Cytometry; D005819:Genetic Markers; D005821:Genetic Techniques; D049452:Green Fluorescent Proteins / Q000378:metabolism; D006801:Humans; D051379:Mice; D008957:Models, Genetic; D009124:Muscle Proteins / Q000235:genetics* / Q000502:physiology*; D009132:Muscles / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D012313:RNA / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D011995:Recombination, Genetic; D018626:Retroelements / Q000235:genetics; D014018:Tissue Distribution
chemical_list: D018076:DNA, Complementary; D005819:Genetic Markers; D009124:Muscle Proteins; D011994:Recombinant Proteins; D018626:Retroelements; D049452:Green Fluorescent Proteins; D003562:Cytidine; D012313:RNA; D000071478:APOBEC Deaminases; D000071480:APOBEC-3G Deaminase; C496166:APOBEC3G protein, mouse; C485629:Apobec2 protein, mouse; C503504:Apobec3 protein, mouse; D003564:Cytidine Deaminase