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Capture Compound Mass Spectrometry - A Powerful Tool to Identify Novel c-di-GMP Effector Proteins

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El tetramérico c-di-GMP media la dimerización efectiva del factor de transcripción para controlar el desarrollo de

Natalia Tschowri¹, Maria A Schumacher², Susan Schlimpert¹

¹Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.

|August 30, 2014

Resumen

El di-GMP cíclico (c-di-GMP) forma un tetramero para dimerizar el factor de transcripción BldD, controlando la esporulación bacteriana. Esto revela un nuevo mecanismo para la dimerización de proteínas mediada por moléculas de señalización.

Área de la Ciencia:

Biología Molecular Biología Molecular
Microbiología Microbiología.
La bioquímica es la bioquímica.

Sus antecedentes:

El di-GMP cíclico (c-di-GMP) es un segundo mensajero crucial que regula diversos procesos celulares.
BldD es un factor de transcripción clave que controla la diferenciación multicelular en las bacterias esporulantes.

Objetivo del estudio:

Para aclarar el mecanismo por el cual c-di-GMP media la dimerización de BldD.
Para investigar las bases estructurales de la interacción c-di-GMP-BldD.

Principales métodos:

Análisis estructural (por ejemplo, cristalografía de rayos X)
Ensayos bioquímicos (por ejemplo, estudios de interacción proteína-proteína)
Mutagénesis dirigida al sitio para identificar los principales motivos de unión.

Principales resultados:

c-di-GMP forma una estructura tetramérica. c-di-GMP forma una estructura tetramérica. c-di-GMP forma una estructura tetramérica. c-di-GMP forma una estructura tetramérica.
Tetrameric c-di-GMP efectivamente une dos subunidades de BldD, lo que permite la dimerización.
La dimerización de BldD es esencial para reprimir los genes de esporulación durante el crecimiento vegetativo.
Un motivo RXD-X8-RXXD específico en BldD media la unión selectiva al tetramero c-di-GMP.

Conclusiones:

c-di-GMP puede adoptar estados oligoméricos alternativos (tetrámeros) para realizar funciones distintas.
Este estudio revela un mecanismo único de señalización de la dimerización de proteínas mediada por moléculas.
Los hallazgos proporcionan información sobre la regulación de la diferenciación bacteriana y la expresión génica.

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