Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes.
Annu Rev Biochem
; 85: 715-42, 2016 Jun 02.
Article
en En
| MEDLINE
| ID: mdl-27050154
Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989, groundbreaking experiments demonstrated that a purified chaperone can bind and prevent the aggregation of artificially unfolded polypeptides and use ATP to dissociate and convert them into native proteins. A decade later, other chaperones were shown to use ATP hydrolysis to unfold and solubilize stable protein aggregates, leading to their native refolding. Presently, the main conserved chaperone families Hsp70, Hsp104, Hsp90, Hsp60, and small heat-shock proteins (sHsps) apparently act as unfolding nanomachines capable of converting functional alternatively folded or toxic misfolded polypeptides into harmless protease-degradable or biologically active native proteins. Being unfoldases, the chaperones can proofread three-dimensional protein structures and thus control protein quality in the cell. Understanding the mechanisms of the cellular unfoldases is central to the design of new therapies against aging, degenerative protein conformational diseases, and specific cancers.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Proteínas HSP70 de Choque Térmico
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Chaperonina 60
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Proteínas Mitocondriales
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Proteínas de Choque Térmico Pequeñas
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Proteínas del Choque Térmico HSP110
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Desplegamiento Proteico
Límite:
Humans
Idioma:
En
Revista:
Annu Rev Biochem
Año:
2016
Tipo del documento:
Article
País de afiliación:
Suiza