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Detection of Protein Ubiquitination

Detection of Protein Ubiquitination

Published on: August 19, 2009

Perspectivas estructurales sobre la ubicación no canónica catalizada por el SidE

Yong Wang¹, Miao Shi¹, Han Feng¹

¹CAS Key Laboratory of Infection and Immunity, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

|May 8, 2018

Resumen

Legionella pneumophila y sus derivados

Área de la Ciencia:

Biología molecular
Biología estructural
La bioquímica

Sus antecedentes:

La ubiquitinación es un proceso clave de señalización eucariota.
La ubiquitinación convencional utiliza una cascada de enzimas E1-E2-E3 dependientes del ATP.
Los efectores de Legionella pneumophila SidE utilizan un nuevo mecanismo de ubiquitinación.

Objetivo del estudio:

Para aclarar el mecanismo molecular de la ubiquitinación no canónica por Legionella SidE.
Determinar la base estructural para la actividad de ubiquitinación única de SidE.

Principales métodos:

Cristalografía de rayos X para determinar las estructuras de SidE solo y en complejo con ubiquitina, NAD y ADP-ribosa.
Ensayos bioquímicos para analizar la actividad enzimática de SidE y el reconocimiento de sustratos.

Principales resultados:

Las estructuras cristalinas capturaron distintas conformaciones de SidE antes y después de la unión del ligando.
Las estructuras revelaron características únicas de la transferencia de ubiquitina por los dominios mART y PDE de SidE.
Los miembros de la familia SidE carecen de reconocimiento específico del pliegue de la proteína del sustrato.

Conclusiones:

SidE emplea una vía de ubiquitinación no canónica independiente de la maquinaria anfitriona.
Los datos estructurales y bioquímicos proporcionan información mecanicista sobre este nuevo sistema de ubiquitinación.
Este trabajo amplía nuestra comprensión de la diversidad de ubiquitinación y los mecanismos efectores bacterianos.

Palabras clave:

ADP-ribosilación ADP-ribosiltransferasa y sus derivados Legionella pneumophila y sus derivados SdeA (en inglés)El lado Interacción huésped-patógeno En el caso de la fosfodiesterasa:La estructura Ubiquitina y sus derivados ubiquitinación

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