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Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Un chaperón molecular de una arquebacterium termofílica está relacionado con la proteína eucariota t-complejo
J D Trent1, E Nimmesgern, J S Wall
1Howard Hughes Medical Institute, Yale School of Medicine, New Haven, Connecticut 06510.
Nature
|December 12, 1991
Resumen
La proteína de choque térmico factor termofílico 55 (TF55) de las arquebacterias actúa como un chaperón molecular. Está relacionado evolutivamente con la proteína eucariota t-complejo polipéptido-1 (TCP1), lo que sugiere una nueva clase de chaperones.
Área de la Ciencia:
- Biología Molecular Biología Molecular
- Biología evolutiva Biología evolutiva.
- La bioquímica es la bioquímica.
Sus antecedentes:
- La evidencia sugiere vínculos evolutivos entre los componentes arqueobacterianos y el citosol eucariótico.
- Las proteínas de choque térmico a menudo funcionan como acompañantes moleculares, ayudando en el plegamiento y la estabilidad de las proteínas.
Objetivo del estudio:
- Investigar la función y la relación evolutiva de la principal proteína de choque térmico (TF55) de la arquebacterium termófila Sulfolobus shibatae.
- Para determinar si TF55 es una chaperona molecular y si se relaciona con los componentes de la chaperona eucariota.
Principales métodos:
- Caracterización de la estructura y el estado oligomérico de TF55.
- Evaluación de la capacidad de TF55 para unirse a polipéptidos desplegados in vitro.
- Analizando la actividad de la ATPasa de TF55.
- Comparando la estructura primaria de TF55 con las chaperonas conocidas y las proteínas eucariotas.
Principales resultados:
- TF55 es un complejo homooligomérico que se asemeja a las estructuras de anillo de la chaperonina.
- TF55 exhibe actividad de chaperona molecular, incluida la unión a polipéptidos desplegados y posee actividad ATPasa.
- La estructura primaria de TF55 no está relacionada con las chaperoninas conocidas, pero muestra una alta homología con la proteína eucariota TCP1.
- TCP1 es esencial en Saccharomyces cerevisiae y está involucrado en la formación del huso mitótico.
Conclusiones:
- TF55 funciona como un acompañante molecular en las arquebacterias termófilas.
- TF55 y el eucariota TCP1 representan una nueva clase de chaperones moleculares, lo que indica una antigua relación evolutiva.
- Este hallazgo amplía nuestra comprensión de la diversidad y la evolución de los acompañantes en diferentes dominios de la vida.
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