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Cation-induced intramolecular coil-to-globule transition in poly(ADP-ribose)

Author

Listed:
  • Tong Wang

    (Cornell University)

  • Kush Coshic

    (University of Illinois Urbana Champaign)

  • Mohsen Badiee

    (Johns Hopkins University)

  • Maranda R. McDonald

    (Johns Hopkins University
    Johns Hopkins University)

  • Aleksei Aksimentiev

    (University of Illinois Urbana Champaign
    University of Illinois Urbana Champaign
    University of Illinois Urbana Champaign)

  • Lois Pollack

    (Cornell University)

  • Anthony K. L. Leung

    (Johns Hopkins University
    Johns Hopkins University
    Johns Hopkins University
    Johns Hopkins University)

Abstract

Poly(ADP-ribose) (PAR), a non-canonical nucleic acid, is essential for DNA/RNA metabolism and protein condensation, and its dysregulation is linked to cancer and neurodegeneration. However, key structural insights into PAR’s functions remain largely uncharacterized, hindered by the challenges in synthesizing and characterizing PAR, which are attributed to its length heterogeneity. A central issue is how PAR, comprised solely of ADP-ribose units, attains specificity in its binding and condensing proteins based on chain length. Here, we integrate molecular dynamics simulations with small-angle X-ray scattering to analyze PAR structures. We identify diverse structural ensembles of PAR that fall into distinct subclasses and reveal distinct compaction of two different lengths of PAR upon the addition of small amounts of Mg2+ ions. Unlike PAR15, PAR22 forms ADP-ribose bundles via local intramolecular coil-to-globule transitions. Understanding these length-dependent structural changes could be central to deciphering the specific biological functions of PAR.

Suggested Citation

  • Tong Wang & Kush Coshic & Mohsen Badiee & Maranda R. McDonald & Aleksei Aksimentiev & Lois Pollack & Anthony K. L. Leung, 2024. "Cation-induced intramolecular coil-to-globule transition in poly(ADP-ribose)," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-51972-9
    DOI: 10.1038/s41467-024-51972-9
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    References listed on IDEAS

    as
    1. Dea Slade & Mark S. Dunstan & Eva Barkauskaite & Ria Weston & Pierre Lafite & Neil Dixon & Marijan Ahel & David Leys & Ivan Ahel, 2011. "The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase," Nature, Nature, vol. 477(7366), pages 616-620, September.
    2. Eva Barkauskaite & Amy Brassington & Edwin S. Tan & Jim Warwicker & Mark S. Dunstan & Benito Banos & Pierre Lafite & Marijan Ahel & Timothy J. Mitchison & Ivan Ahel & David Leys, 2013. "Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities," Nature Communications, Nature, vol. 4(1), pages 1-8, October.
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