Polyphosphate is a primordial chaperone.
Mol Cell
; 53(5): 689-99, 2014 Mar 06.
Article
em En
| MEDLINE
| ID: mdl-24560923
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Polifosfatos
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Chaperonas Moleculares
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Proteínas de Escherichia coli
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Escherichia coli
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article