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Una proteína Fos que contiene la cremallera de leucina de Jun forma un homodímero que se une al sitio de unión AP1
M Neuberg1, J Adamkiewicz, J B Hunter
1Institut für Molekularbiologie und Tumorforschung, Phillipps-Universität Marburg, FRG.
Nature
|September 21, 1989
Resumen
El estudio revela que la modificación de la proteína Fos
Área de la Ciencia:
- Biología Molecular Biología Molecular
- Genética La genética.
- La bioquímica es la bioquímica.
Sus antecedentes:
- El elemento sensible al TPA (TRE) está unido por el factor de transcripción AP1, un complejo de proteínas Fos y Jun.
- Tanto las proteínas Fos como las Jun contienen una estructura de cremallera de leucina esencial para su interacción.
- Una región básica cerca de la cremallera de leucina en Fos es crítica para la unión del ADN.
Objetivo del estudio:
- Para investigar el papel de la cremallera de leucina en las interacciones de las proteínas Fos y Jun y la unión al ADN.
- Para determinar si Fos contribuye específicamente al reconocimiento de TRE.
- Para probar la hipótesis de un sitio simétrico de unión del ADN en el complejo Fos-Jun.
Principales métodos:
- Se utilizó la mutagénesis dirigida al sitio para alterar las estructuras de las proteínas.
- Una proteína quimérica, psi-Fos, fue diseñada mediante el intercambio de la cremallera de leucina de Fos con la de Jun.
- Se evaluaron las afinidades de unión de los homodímeros Fos-psi-Fos y psi-Fos con el TRE.
Principales resultados:
- La proteína psi-Fos diseñada podría formar complejos con el Fos.
- El heterodímero Fos-psi-Fos y, en menor medida, el homodímero psi-Fos específicamente unido al TRE.
- Esto indica que la región de la cremallera de leucina es crucial para la unión específica del ADN.
Conclusiones:
- Los hallazgos apoyan el modelo de un sitio de unión de ADN casi simétrico formado por proteínas Fos y Jun que interactúan con el TRE. palindromo.
- El intercambio de cremalleras de leucina demuestra su papel crítico en la mediación del reconocimiento específico del ADN.
- Esta investigación aclara el mecanismo de unión cooperativa del factor de transcripción AP1.
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