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ADAR proteins: double-stranded RNA and Z-DNA binding domains
Pierre Barraud1, Frédéric H-T Allain
1Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zürich, Switzerland.
Current Topics in Microbiology and Immunology
|July 6, 2011
Summary
Adenosine deaminases acting on RNA (ADAR) enzymes modify RNA by changing adenosine to inosine. This RNA editing process generates protein diversity by altering codons and splice sites.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Adenosine deaminases acting on RNA (ADAR) are enzymes crucial for RNA editing.
- ADARs catalyze the conversion of adenosine to inosine within double-stranded RNA (dsRNA) substrates.
- This editing process can alter protein-coding sequences and splicing patterns.
Purpose of the Study:
- To review the current structural and molecular understanding of RNA editing by the ADAR protein family.
- To focus on the dsRNA and Z-DNA binding domains within ADAR proteins.
Main Methods:
- Literature review of structural and molecular data on ADAR proteins.
- Analysis of the known functions of dsRNA and Z-DNA binding domains in ADARs.
Main Results:
- ADAR-mediated RNA editing introduces molecular diversity by altering RNA sequences.
- Inosine, resulting from adenosine editing, is typically recognized as guanine by cellular machinery.
- Changes can lead to altered amino acid sequences, premature stop codons, or new splice sites, enhancing proteome diversity from a single gene.
Conclusions:
- ADAR enzymes play a significant role in generating functional diversity within the proteome.
- Understanding the structural and molecular mechanisms of ADARs, particularly their binding domains, is key to comprehending their biological impact.
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