Comprehensive interrogation of the ADAR2 deaminase domain for engineering enhanced RNA editing activity and specificity

Elife. 2022 Jan 19:11:e75555. doi: 10.7554/eLife.75555.

Abstract

Adenosine deaminases acting on RNA (ADARs) can be repurposed to enable programmable RNA editing, however their exogenous delivery leads to transcriptome-wide off-targeting, and additionally, enzymatic activity on certain RNA motifs, especially those flanked by a 5' guanosine is very low thus limiting their utility as a transcriptome engineering toolset. Towards addressing these issues, we first performed a novel deep mutational scan of the ADAR2 deaminase domain, directly measuring the impact of every amino acid substitution across 261 residues, on RNA editing. This enabled us to create a domain-wide mutagenesis map while also revealing a novel hyperactive variant with improved enzymatic activity at 5'-GAN-3' motifs. As overexpression of ADAR enzymes, especially hyperactive variants, can lead to significant transcriptome-wide off-targeting, we next engineered a split-ADAR2 deaminase which resulted in >100-fold more specific RNA editing as compared to full-length deaminase overexpression. Taken together, we anticipate this systematic engineering of the ADAR2 deaminase domain will enable broader utility of the ADAR toolset for RNA biotechnology applications.

Keywords: ADARs; RNA editing; biochemistry; chemical biology; computational biology; deep mutational scan; human; split proteins; systems biology.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Deaminase / genetics*
  • Adenosine Deaminase / metabolism
  • Humans
  • Nucleotide Motifs
  • Protein Domains
  • Protein Engineering
  • RNA Editing*
  • RNA-Binding Proteins / genetics*
  • RNA-Binding Proteins / metabolism
  • Transcriptome*

Substances

  • RNA-Binding Proteins
  • ADARB1 protein, human
  • Adenosine Deaminase

Associated data

  • GEO/GSE158656