Identification of ADAR1 p150 and p110 Associated Edit Sites

Tony Sun; Brad R Rosenberg; Hachung Chung; Charles M Rice

doi:10.1007/978-1-0716-3084-6_20

Identification of ADAR1 p150 and p110 Associated Edit Sites

Methods Mol Biol. 2023:2651:285-294. doi: 10.1007/978-1-0716-3084-6_20.

Authors

Tony Sun¹, Brad R Rosenberg², Hachung Chung³, Charles M Rice⁴

Affiliations

¹ Laboratory of Virology and Infectious Disease, The Rockefeller University, New York, NY, USA. tony_sun@urmc.rochester.edu.
² Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
³ Department of Microbiology and Immunology, Columbia University, New York, NY, USA.
⁴ Laboratory of Virology and Infectious Disease, The Rockefeller University, New York, NY, USA.

PMID: 36892775
DOI: 10.1007/978-1-0716-3084-6_20

Abstract

Adenosine deaminase acting on RNA 1 (ADAR1) catalyzes adenosine-to-inosine editing on double-stranded RNA molecules and is involved in regulating cellular responses to endogenous and exogenous RNA. ADAR1 is the primary A-to-I editor of RNA in humans, and the majority of edit sites are found in a class of short interspersed nuclear elements called Alu elements, many of which are located in introns and 3' untranslated regions. Two ADAR1 protein isoforms, p110 (110 kDa) and p150 (150 kDa), are known to be coupled in expression, and decoupling the expression of these isoforms has revealed that the p150 isoform edits a broader range of targets compared to p110. Numerous methods for identification of ADAR1-associated edits have been developed, and we present here a specific method for identification of edit sites associated with individual ADAR1 isoforms.

Keywords: A-to-I editing; ADAR1; RNA sequencing.

MeSH terms

Adenosine Deaminase* / metabolism
Humans
Introns
Protein Isoforms / genetics
RNA, Double-Stranded*

Substances

Adenosine Deaminase
Protein Isoforms
RNA, Double-Stranded
ADAR protein, human