Selective Recognition of RNA Substrates by ADAR Deaminase Domains

• Published in: Biochemistry (Easton) Vol. 57; no. 10; pp. 1640 - 1651
• Main Authors: Wang, Yuru, Park, SeHee, Beal, Peter A
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 13.03.2018
• Subjects: adenosine; Adenosine Deaminase - chemistry; Adenosine Deaminase - metabolism; Base Sequence; deamination; essential amino acids; fluorescence; Genes, Reporter; Green Fluorescent Proteins - genetics; High-Throughput Screening Assays; Humans; messenger RNA; mutagenesis; Protein Domains; Protein Processing, Post-Translational; recombinant fusion proteins; RNA - chemistry; RNA - metabolism; RNA editing; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - metabolism; Saccharomyces cerevisiae; sequence analysis; Sequence Analysis, RNA; Substrate Specificity; transcriptome

Adenosine deamination is one of the most prevalent post-transcriptional modifications in mRNA and is catalyzed by ADAR1 and ADAR2 in humans. ADAR1 and ADAR2 have different substrate selectivity, which is believed to mainly originate from the proteins’ deaminase domains (hADAR1d and hADAR2d, respecti...