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Assaying for Inorganic Polyphosphate in Bacteria
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Polyphosphate is a primordial chaperone.

Michael J Gray1, Wei-Yun Wholey2, Nico O Wagner1

  • 1Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.

Molecular Cell
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Inorganic polyphosphate (polyP) acts as a novel chaperone, stabilizing proteins and protecting them from stress. This ancient molecule aids protein folding, suggesting a primordial role in cellular protection.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Stress Response

Background:

  • Inorganic polyphosphate (polyP) is an ancient, conserved molecule composed of phosphate monomers.
  • The biological functions of polyP remain largely enigmatic despite its prevalence.

Purpose of the Study:

  • To investigate the potential chaperone activity of inorganic polyphosphate (polyP).
  • To elucidate the role of polyP in protein stabilization and protection under proteotoxic stress.

Main Methods:

  • In vivo studies assessing protein stabilization and survival under stress conditions.
  • In vitro experiments measuring polyP's interaction with unfolding proteins and its effect on refolding.
  • Assays for ATP-independent binding and high-affinity interactions with denatured proteins.

Main Results:

  • PolyP demonstrates significant in vivo protein stabilization, reducing reliance on other chaperone systems.
  • PolyP protects diverse proteins against stress-induced unfolding and aggregation.
  • In vitro, polyP exhibits chaperone-like qualities, binding unfolding proteins and promoting refolding.

Conclusions:

  • Inorganic polyphosphate (polyP) functions as a previously unrecognized protein chaperone.
  • PolyP plays a critical role in cellular proteostasis and stress resilience.
  • PolyP may represent one of nature's earliest chaperone molecules with enduring biological relevance.