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Conservación evolutiva de los componentes del complejo de translocación de proteínas

E Hartmann¹, T Sommer, S Prehn

¹Max-Delbrück Centre for Molecular Medicine, Berlin-Buch, Germany.

|February 17, 1994

Resumen

El complejo Sec61p facilita el transporte de proteínas hacia el retículo endoplasmático. Su subunidad gamma es homóloga a las proteínas bacterianas, lo que sugiere un papel conservado en la translocación de proteínas en todos los organismos.

Área de la Ciencia:

Biología Molecular Biología Molecular
Biología celular Biología celular.
La bioquímica es la bioquímica.

Sus antecedentes:

La translocación de proteínas en el retículo endoplasmático es vital para la función celular.
El complejo Sec61p de mamíferos, compuesto por tres proteínas de membrana, media este proceso.
Los homólogos de Sec61p, como el bacteriano SecYp, están involucrados en la exportación de proteínas.

Objetivo del estudio:

Para determinar las secuencias de las subunidades beta y gamma del complejo Sec61p de mamíferos.
Investigar las relaciones funcionales y estructurales entre los componentes de translocación de proteínas de mamíferos y bacterias.

Principales métodos:

La secuenciación de proteínas.
Ensayos de complementación funcional en levaduras.
Análisis de homología estructural Análisis de homología estructural.

Principales resultados:

Se determinaron las secuencias de las subunidades beta y gamma Sec61p de mamíferos.
El Sec61-gamma de mamíferos reemplazó funcionalmente a la levadura SSS1p.
Sec61-gamma y SSS1p mostraron similitud estructural con el SecEp. bacteriano.

Conclusiones:

Las subunidades del complejo Sec61p se conservan en todas las especies.
Al menos dos subunidades del complejo Sec61/SecYp son fundamentales para la translocación de proteínas en todos los organismos.

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