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La espectroscopia de fuerza de una sola molécula revela el diseño mecánico que rige la translocación eficiente de la

Han Wang¹, Xiaoqing Gao², Hongbin Li¹

¹Department of Chemistry , University of British Columbia , Vancouver , British Columbia V6T 1Z1 , Canada.

Journal of the American Chemical Society

|December 3, 2019

Resumen

La translocación de la toxina adenilato ciclasa (CyaA) bacteriana es ayudada por su dominio RTX

Área de la Ciencia:

Secreción de toxinas bacterianas
Dinámica del plegamiento de las proteínas
Biofísica de una sola molécula

Sus antecedentes:

La toxina adenilato ciclasa (CyaA) requiere una translocación eficiente a través del sistema de secreción de tipo 1 (T1SS) para funcionar.
Comprender las propiedades mecánicas del dominio RTX de CyaA es clave para dilucidar los mecanismos de translocación.

Objetivo del estudio:

Investigar las propiedades mecánicas y la dinámica conformacional del dominio RTX de CyaA a nivel de una sola molécula.
Elucidar el papel del plegamiento del dominio RTX en la translocación de CyaA por el T1SS.

Principales métodos:

Utilizó pinzas ópticas para sondear dominios RTX individuales.
Análisis de la estabilidad mecánica y las vías de plegado de los dominios apo- y holo-RTX.

Principales resultados:

El dominio Apo-RTX se comporta como una bobina aleatoria, facilitando la translocación sin resistencia entálpica.
El dominio holo-RTX plegado exhibe estabilidad mecánica y se somete a plegamiento vectorial y cotranslacional desde el extremo C.
El plegamiento desencadenado por Ca2+ de holo-RTX genera una fuerza de estiramiento, ayudando a la translocación de RTX.

Conclusiones:

El plegamiento desencadenado por Ca2+ del dominio RTX juega un papel crucial en la translocación de CyaA.
Se proporcionan conocimientos mecanicistas sobre el diseño mecánico que rige la translocación eficiente de RTX.

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