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RNA sequestration driven by amyloid formation: the alpha synuclein case.

Jakob Rupert1,2, Michele Monti1, Elsa Zacco1

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RNA addition accelerates protein aggregation, particularly for alpha-synuclein mutants with higher RNA-binding affinity. This suggests RNA sequestration is a common gain-of-function mechanism in protein aggregation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Computational Biology

Background:

  • Nucleic acids, particularly RNA, can modulate protein aggregation.
  • Amyloid aggregation involves hydrophobic cores and disordered external regions interacting with nucleic acids.

Purpose of the Study:

  • To computationally characterize physico-chemical properties of protein aggregation regions.
  • To investigate the role of RNA in alpha-synuclein aggregation.

Main Methods:

  • Computational analysis of protein aggregation regions.
  • In vitro aggregation assays with alpha-synuclein (wild-type and C-terminal mutant) and RNA.
  • Assessment of nucleic acid sequestration by aggregated proteins.

Main Results:

  • Disordered protein regions show a tendency to interact with nucleic acids.
  • RNA addition accelerated aggregation for both alpha-synuclein variants.
  • A C-terminal truncated mutant (aS103) exhibited a stronger RNA-induced aggregation acceleration and enhanced RNA sequestration compared to wild-type (aS140).

Conclusions:

  • RNA sequestration is a potential common mechanism in protein aggregation.
  • This RNA sequestration represents a gain-of-function phenomenon in protein aggregation processes.