ADAR enzyme and miRNA story: a nucleotide that can make the difference

Adenosine deaminase acting on RNA (ADAR) enzymes convert adenosine (A) to inosine (I) in double-stranded (ds) RNAs. Since Inosine is read as Guanosine, the biological consequence of ADAR enzyme activity is an A/G conversion within RNA molecules. A-to-I editing events can occur on both coding and non...

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Bibliographic Details
Published in:International Journal of Molecular Sciences 2013-11, Vol.14 (11), p.22796-22816
Main Authors: Tomaselli, Sara, Bonamassa, Barbara, Alisi, Anna, Nobili, Valerio, Locatelli, Franco, Gallo, Angela
Format: Article
Language:English
Subjects:
A-to-I RNA editing
Adenosine - genetics
Adenosine Deaminase - genetics
Adenosine deaminase acting on RNA (ADAR)
double-stranded RNA (dsRNA)
Gene Expression Regulation - genetics
Humans
Inosine - genetics
microRNA
MicroRNAs - genetics
non-coding sequence
Protein Biosynthesis
Review
RNA, Double-Stranded - genetics
RNA-Binding Proteins
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Summary:Adenosine deaminase acting on RNA (ADAR) enzymes convert adenosine (A) to inosine (I) in double-stranded (ds) RNAs. Since Inosine is read as Guanosine, the biological consequence of ADAR enzyme activity is an A/G conversion within RNA molecules. A-to-I editing events can occur on both coding and non-coding RNAs, including microRNAs (miRNAs), which are small regulatory RNAs of ~20-23 nucleotides that regulate several cell processes by annealing to target mRNAs and inhibiting their translation. Both miRNA precursors and mature miRNAs undergo A-to-I RNA editing, affecting the miRNA maturation process and activity. ADARs can also edit 3' UTR of mRNAs, further increasing the interplay between mRNA targets and miRNAs. In this review, we provide a general overview of the ADAR enzymes and their mechanisms of action as well as miRNA processing and function. We then review the more recent findings about the impact of ADAR-mediated activity on the miRNA pathway in terms of biogenesis, target recognition, and gene expression regulation.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms141122796