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Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
Published on: January 5, 2024
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Nucleic acid actions on abnormal protein aggregation, phase transitions and phase separation.
Jerson L Silva1, Tuane C Vieira1, Yraima Cordeiro2
1Institute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ, 21941-901, Brazil.
Current Opinion in Structural Biology
|March 5, 2022
Summary
Protein phase separation and transitions are linked to conformational diseases. Nucleic acids modulate these processes in amyloidogenic proteins like PrP and p53, impacting their function and pathology.
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- Liquid-liquid phase separation (LLPS) and phase transitions (PT) are physical processes implicated in conformational diseases.
- Nucleic acid (NA)-binding proteins involved in neurodegenerative disorders and cancer undergo PT modulated by NAs.
Purpose of the Study:
- To discuss recent work on phase separation and transitions of two amyloidogenic proteins: prion protein (PrP) and p53.
- To explore the role of different NAs in these processes.
Main Methods:
- Review of recent studies on protein phase separation and transitions.
- Analysis of NA-protein interactions and their impact on protein conformational changes and aggregation.
Main Results:
- Amyloidogenic proteins, PrP and p53, undergo phase transitions upon NA interaction.
- Different NAs modulate the phase behavior of these proteins, influencing conformational changes and aggregation.
Conclusions:
- Phase separation and transitions are relevant to both the functional and pathological roles of mammalian proteins like PrP and p53.
- Understanding NA-modulated PTs is crucial for elucidating disease mechanisms in neurodegeneration and cancer.
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