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Polyphosphate Is a Primordial Chaperone

2014; Elsevier BV; Volume: 53; Issue: 5 Linguagem: Inglês

10.1016/j.molcel.2014.01.012

1097-4164

Michael J. Gray, Wei‐Yun Wholey, Nico Wagner, Claudia M. Cremers, Antje Mueller-Schickert, Nathaniel T. Hock, Adam Krieger, Erica M. Smith, R. Bender, James C.A. Bardwell, Ursula Jakob,

Enzyme function and inhibition

Summary 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 in vivo, 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. In vitro 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.