the aidapobec family of nucleic acid mutators核酸的aidapobec家族调整器.pdfVIP

Protein family review TThhee AAIIDD//AAPPOOBBEECC ffaammiillyy ooff nnuucclleeiicc aacciidd mmuuttaattoorrss Silvestro G Conticello Address: Core Research Laboratory - Istituto Toscano Tumori, Florence, Via Cosimo il Vecchio 2, 50139 Firenze, Italy. Email: silvo.conticello@ittumori.it Published: 17 June 2008 Genome BBiioollooggyy 2008, 99::229 (doi:10.1186/gb-2008-9-6-229) The electronic version of this article is the complete one and can be found online at /2008/9/6/229 © 2008 BioMed Central Ltd SSuummmmaarryy The AID/APOBECs, a group of cytidine deaminases, represent a somewhat unusual protein family that can insert mutations in DNA and RNA as a result of their ability to deaminate cytidine to uridine. The ancestral AID/APOBECs originated from a branch of the zinc-dependent deaminase superfamily at the beginning of the vertebrate radiation. Other members of the family have arisen in mammals and present a history of complex gene duplications and positive selection. All AID/APOBECs have a characteristic zinc-coordination motif, which forms the core of the catalytic site. The crystal structure of human APOBEC2 shows remarkable similarities to that of the bacterial tRNA-editing enzyme TadA, which suggests a conserved mechanism by which polynucleotides are recognized and deaminated. The AID/APOBECs seem to have diverse roles. AID and the APOBEC3s are DNA mutators, acting in antigen-driven antibody diversification processes and in an innate defense system against retroviruses, respectively. APOBEC1 edits the mRNA for apolipoprotein B, a protein involved in lipid transport. A detailed understanding of the