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Stress-Induced Low Complexity RNA Activates Physiological Amyloidogenesis.
Miling Wang1, Xianzun Tao2, Mathieu D Jacob3
1Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL 33136, USA; Sylvester Comprehensive Cancer Center, Miller School of Medicine, University of Miami, Miami, FL 33136, USA; Department of Urology, Miller School of Medicine, University of Miami, Miami, FL 33136, USA.
Cell Reports
|August 16, 2018
Summary
Stimulus-induced amyloid bodies (A-bodies) form via RNA architectural determinants. Low-complexity RNA sequences recruit diverse proteins, initiating A-body formation and highlighting the function of repetitive genomic regions.
Area of Science:
- Molecular Biology
- Genomics
- Cell Biology
Background:
- Amyloid bodies (A-bodies) are inducible, membrane-less nuclear compartments.
- A-bodies are protein aggregates adopting an amyloid-like state.
- Noncoding RNA from rDNA intergenic spacer (rIGSRNA) seeds A-body formation.
Purpose of the Study:
- To investigate the mechanism by which rIGSRNA recruits diverse proteins to form A-bodies.
- To identify the architectural determinants of rIGSRNA responsible for protein recruitment.
Main Methods:
- Analysis of RNA structure and sequence.
- Biochemical assays to study protein-RNA interactions.
- Cellular imaging to observe A-body formation in the nucleolus.
Main Results:
- Long, low-complexity dinucleotide repeats (CU or AG) in rIGSRNA act as architectural determinants.
- These repeats facilitate charge-based interactions with cationic peptides, forming liquid-like nucleolar foci.
- High local concentrations of fibrillation-prone proteins within these foci drive the formation of an amyloidogenic liquid phase, seeding A-bodies.
Conclusions:
- Low-complexity RNA sequences and repetitive genomic regions play a crucial role in A-body biogenesis.
- These findings underscore the functional significance of previously overlooked genomic elements.
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