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In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
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Plasticidad estructural de la ubiquitina ligasa D3-D14 en la señalización de las estrigolactonas
Nitzan Shabek1,2,3, Fabrizio Ticchiarelli4, Haibin Mao1,2
1Department of Pharmacology, University of Washington, Seattle, WA, USA.
Nature
|November 23, 2018
Resumen
Las hormonas vegetales llamadas estrigolactonas regulan el crecimiento de las plantas. La interacción entre la enzima D14 y la proteína D3, controlada por las estrigolactonas, conduce a la degradación del represor D53, inhibiendo la ramificación de los brotes.
Área de la Ciencia:
- La señalización de las hormonas vegetales
- Fisiología molecular de las plantas
- Ubiquitinación de las proteínas
Sus antecedentes:
- Las estrigolactonas son hormonas vegetales cruciales que regulan diversos procesos fisiológicos.
- La hidrolasa D14 metaboliza las estrigolactonas e interactúa con la proteína de la caja F D3.
- Esta interacción se dirige al represor de transcripción D53 para la ubiquitinación y degradación, inhibiendo la ramificación de los brotes.
Objetivo del estudio:
- Para aclarar el mecanismo de la ubiquitinación D53 dependiente de las hormonas mediada por D14 y D3.
- Para entender cómo funciona D14 con D3 en la señalización de la estrigolactona.
- Para revelar la base estructural de la interacción entre D14, D3 y D53.
Principales métodos:
- Análisis estructural de la proteína D3.
- Ensayos bioquímicos para estudiar las interacciones proteína-proteína.
- Investigación de la modulación de la actividad enzimática.
- Análisis de la ubiquitinación dependiente de la estrigolactona.
Principales resultados:
- La proteína D3 posee una hélice α terminal C con dos estados conformacionales distintos.
- El estado "engajado" facilita la unión de D3, D14 y un intermediario de estrigolactona hidrolizado.
- El estado "desalojado" se une al D14 no modificado, inhibiendo su actividad enzimática, y permite el reclutamiento de D53 dependiente de la estrigolactona.
- Esto revela la plasticidad estructural de la ubiquitina ligasa SCF D3-D14.
Conclusiones:
- La flexibilidad conformacional de la hélice α terminal C de D3 es clave para coordinar la señalización y el metabolismo de la estrigolactona.
- Se propone un mecanismo en el que la actividad de la ligasa E3 está regulada por la unión a la estrigolactona y las interacciones con las proteínas.
- Este estudio proporciona información estructural sobre una vía crítica de señalización de hormonas vegetales.
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