Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity

Matthews, Melissa M.; Thomas, Justin M.; Zheng, Yuxuan; Tran, Kiet; Phelps, Kelly J.; Scott, Anna I.; Havel, Jocelyn; Fisher, Andrew J.; Beal, Peter A.

doi:10.1038/nsmb.3203

Title: Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity

Journal Article · Mon Apr 11 00:00:00 EDT 2016 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/nsmb.3203· OSTI ID:1255288

Matthews, Melissa M. ^[1]; Thomas, Justin M. ^[1]; Zheng, Yuxuan ^[1]; Tran, Kiet ^[1]; Phelps, Kelly J. ^[1]; Scott, Anna I. ^[2]; Havel, Jocelyn ^[1]; Fisher, Andrew J. ^[3]; Beal, Peter A. ^[1]

Univ. of California, Davis, CA (United States). Dept. of Chemistry
Univ. of California, Davis, CA (United States). Dept. of Molecular and Cellular Biology
Univ. of California, Davis, CA (United States). Dept. of Chemistry. Dept. of Molecular and Cellular Biology

Adenosine deaminases acting on RNA (ADARs) are editing enzymes that convert adenosine to inosine in duplex RNA, a modification reaction with wide-ranging consequences in RNA function. Understanding of the ADAR reaction mechanism, the origin of editing-site selectivity, and the effect of mutations is limited by the lack of high-resolution structural data for complexes of ADARs bound to substrate RNAs. In this paper, we describe four crystal structures of the human ADAR2 deaminase domain bound to RNA duplexes bearing a mimic of the deamination reaction intermediate. These structures, together with structure-guided mutagenesis and RNA-modification experiments, explain the basis of the ADAR deaminase domain's dsRNA specificity, its base-flipping mechanism, and its nearest-neighbor preferences. In addition, we identified an ADAR2-specific RNA-binding loop near the enzyme active site, thus rationalizing differences in selectivity observed between different ADARs. In conclusion, our results provide a structural framework for understanding the effects of ADAR mutations associated with human disease.

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Research Organization:: Univ. of California, Davis, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Inst. of Health (NIH) (United States)

Grant/Contract Number:: AC02-06CH11357; AC02-76SF00515; R01GM061115; T32 GM007377; P41GM103393; P41 GM103403; S10 RR029205

OSTI ID:: 1255288

Journal Information:: Nature Structural & Molecular Biology, Vol. 23, Issue 5; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 124 works

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