Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 43, Issue 8, Pages 606-622Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2018.04.013
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Funding
- PHS [R21NS067671, R21AI095007, R21AI122845, R01GM110038, R01GM110568]
- Bill and Melinda Gates Fund Grand Challenges Explorations [51715]
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The 11-member APOBEC (apolipoprotein B mRNA editing catalytic polypeptide-like) family of zinc-dependent cytidine deaminases bind to RNA and single-stranded DNA (ssDNA) and, in specific contexts, modify select (deoxy) cytidines to (deoxy) uridines. In this review, we describe advances made through high-resolution co-crystal structures of APOBECs bound to mono-or oligonucleotides that reveal potential substrate-specific binding sites at the active site and non-sequence-specific nucleic acid binding sites distal to the active site. We also discuss the effect of APOBEC oligomerization on functionality. Future structural studies will need to address how ssDNA binding away from the active site may enhance catalysis and the mechanism by which RNA binding may modulate catalytic activity on ssDNA.
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