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Switch-like compaction of poly(ADP-ribose) upon cation binding.

Mohsen Badiee1, Adam L Kenet1, Laura R Ganser2

  • 1Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205.

Proceedings of the National Academy of Sciences of the United States of America
|May 1, 2023
PubMed
Summary

Poly(ADP-ribose) (PAR) is stiff and compacts like a switch when cations bind. This cation-driven compaction may explain how PAR recognizes specific molecules in cells.

Keywords:
PAR-binding proteinpersistence lengthpoly(ADP-ribose)single molecule FRET

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Poly(ADP-ribose) (PAR) is a posttranslational modification regulating cellular processes.
  • PAR acts as a scaffold in macromolecular complexes and biomolecular condensates.
  • The mechanism of PAR's specific molecular recognition remains unclear.

Purpose of the Study:

  • To investigate the flexibility of PAR under varying cation conditions.
  • To understand how cations influence PAR structure and compaction.
  • To elucidate the role of PAR stiffness in molecular recognition.

Main Methods:

  • Single-molecule fluorescence resonance energy transfer (smFRET) was employed.
  • PAR flexibility was evaluated across different cation concentrations and valencies (Na+, Mg2+, Ca2+, spermine4+).
  • The effect of the intrinsically disordered protein FUS on PAR compaction was assessed.

Main Results:

  • PAR exhibits a longer persistence length compared to RNA and DNA.
  • PAR undergoes a sharp transition from extended to compact states upon cation binding.
  • The degree of PAR compaction is dependent on cation concentration and valency.
  • The protein FUS also induced PAR compaction, acting as a macromolecular cation.

Conclusions:

  • PAR molecules possess inherent stiffness.
  • Cation binding triggers switch-like compaction of PAR.
  • The cationic environment is a key factor driving PAR recognition specificity.