Z-DNA and Z-RNA in human disease
By A. Herbert. 2019
159 citations recorded by the source corpus.
Left-handed Z-DNA/Z-RNA is bound with high affinity by the Zα domain protein family that includes ADAR (a double-stranded RNA editing enzyme), ZBP1 and viral orthologs regulating innate immunity. Loss-of-function mutations in ADAR p150 allow persistent activation of the interferon system by Alu dsRNAs and are causal for Aicardi-Goutières Syndrome. Heterodimers of ADAR and DICER1 regulate the switch from RNA- to protein-centric immunity. Loss of DICER1 function produces age-related macular degeneration, a different type of Alu-mediated disease. The overlap of Z-forming sites with those for the signal recognition particle likely limits invasion of primate genomes by Alu retrotransposons.Alan Herbert discusses the properties of Z-DNA and Z-RNA, interactions with ADAR and other Z-binding proteins, and the role these elements play in disease. He also discusses the implication of Z-forming sites in genome evolution.
Subfields: Molecular Biology
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In Molecular Biology
- Tom L. Blundell
- Yang Zhang
- David B. Ascher
- Douglas E. V. Pires
- Arne Elofsson
- Andrej Sali
- Björn Wallner
- Carlos H. M. Rodrigues
Citations in the corpus
- Searching for New Z-DNA/Z-RNA Binding Proteins Based on Structural Similarity to Experimentally Validated Zα Domain (2022, background): “Negative supercoiling of DNA and protein binding can increase the stability of local DNA conformation and/or induce conformational changes that give rise to various alternative DNA structures, the best-described being cruciforms [7], Z-DNA/Z-RNA [9,10], triplexes [11] and quadruplexes [12].”