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The structure of APOBEC1 and insights into its RNA and DNA substrate selectivity

Wolfe, Aaron D, Li, Shuxing, Goedderz, Cody, Chen, Xiaojiang S·2020·NAR Cancer
DOI 10.1093/narcan/zcaa027PMC PMC7556403
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Abstract

APOBEC1 (APO1), a member of AID/APOBEC nucleic acid cytosine deaminase family, can edit apolipoprotein B mRNA to regulate cholesterol metabolism. This APO1 RNA editing activity requires a cellular cofactor to achieve tight regulation. However, no cofactors are required for deamination on DNA by APO1 and other AID/APOBEC members, and aberrant deamination on genomic DNA by AID/APOBEC deaminases has been linked to cancer. Here, we present the crystal structure of APO1, which reveals a typical APOBEC deaminase core structure, plus a unique well-folded C-terminal domain that is highly hydrophobic. This APO1 C-terminal hydrophobic domain (A1HD) interacts to form a stable dimer mainly through hydrophobic interactions within the dimer interface to create a four-stranded β-sheet positively charged surface. Structure-guided mutagenesis within this and other regions of APO1 clarified the importance of the A1HD in directing RNA and cofactor interactions, providing insights into the structural basis of selectivity on DNA or RNA substrates.

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Metadata

Authors
Wolfe, A. D., Li, S., Goedderz, C., & Chen, X. S.
Affiliations
  • Genetics, Molecular and Cellular Biology, Keck School of Medicine, University of Southern California, Los Angeles, CA 90089, USA
  • Molecular and Computational Biology, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA
ORCID
Venue
NAR Cancer
Publisher
Oxford University Press (OUP)
Published
2020-10-09
Volume
2
Issue
4
ISSN
2632-8674
DOI
10.1093/narcan/zcaa027
PMC
PMC7556403
Cited by
28
References
1
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
National Institutes of Health (R01 AI150524)

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