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S. cerevisiae codifica una proteína esencial homóloga en secuencia y función a la BiP de mamíferos

K Normington¹, K Kohno, Y Kozutsumi

¹Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.

|June 30, 1989

Resumen

La proteína BiP de los mamíferos ayuda al plegamiento de las proteínas secretoras. El BiP de la levadura, esencial para el crecimiento celular, es idéntico al KAR2, lo que sugiere que la deficiencia de BiP causa un mal plegamiento generalizado de proteínas en el retículo endoplasmático.

Área de la Ciencia:

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

Sus antecedentes:

El retículo endoplasmático (ER) alberga la proteína 78 kd (BiP) en las células de mamíferos, crucial para el plegamiento de las proteínas secretoras y transmembranares.
BiP actúa como un chaperón molecular, facilitando la conformación proteica adecuada dentro de la ER.

Objetivo del estudio:

Para investigar el gen homólogo del BiP de ratón en S. cerevisiae.
Comprender la función y la esencialidad de la levadura BiP en los procesos celulares.

Principales métodos:

Aislamiento del gen homólogo que codifica el BiP de la levadura utilizando el cDNA BiP de un ratón.
Análisis de secuencia que compara la BiP de levadura y ratón.
Estudios complementarios que expresan BiP de mamíferos en mutantes de S. cerevisiae KAR2.

Principales resultados:

Se aisló un gen BiP de levadura, que codifica 682 aminoácidos, de los cuales 431 son idénticos al BiP del ratón.
El BiP de levadura es un gen similar al HSP70, regulado transcripcionalmente por polipéptidos desplegados en el ER.
El gen BiP de la levadura es idéntico al gen KAR2 y es esencial para el crecimiento celular.
La expresión de BiP en mamíferos complementó a un mutante KAR2 sensible a la temperatura.

Conclusiones:

El BiP de levadura juega un papel crítico en la viabilidad celular y es homólogo al BiP de mamíferos.
Las deficiencias en BiP pueden conducir a una falla generalizada de plegamiento de proteínas en la ER.
Los defectos de plegamiento de la proteína ER pueden dar lugar a efectos pleiotrópicos en el metabolismo celular.

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