Polyphosphate Is a Primordial Chaperone

Academic Article


  • Composed of up to 1,000 phospho-anhydride bond-linked phosphate monomers, inorganic polyphosphate (polyP) is one of the most ancient, conserved, and enigmatic molecules in biology. Here we demonstrate that polyP functions as a hitherto unrecognized chaperone. We show that polyP stabilizes proteins invivo, diminishes the need for other chaperone systems to survive proteotoxic stress conditions, and protects a wide variety of proteins against stress-induced unfolding and aggregation. Invitro studies reveal that polyP has protein-like chaperone qualities, binds to unfolding proteins with high affinity in an ATP-independent manner, and supports their productive refolding once nonstress conditions are restored. Our results uncover a universally important function for polyP and suggest that these long chains of inorganic phosphate may have served as one of nature's first chaperones, a role that continues to the present day. © 2014 Elsevier Inc.
  • Authors

    Published In

  • Molecular Cell  Journal
  • Digital Object Identifier (doi)

    Author List

  • Gray MJ; Wholey WY; Wagner NO; Cremers CM; Mueller-Schickert A; Hock NT; Krieger AG; Smith EM; Bender RA; Bardwell JCA
  • Start Page

  • 689
  • End Page

  • 699
  • Volume

  • 53
  • Issue

  • 5