- Se detectaron especies adicionales correspondientes a la proteína PhoQ cuando las cepas de Salmonella son crecidas en presencia de ácido linoleico.
- Se comprobró que la expresión heteróloga de His-PhoQ en células de E. coli
crecidas en medio LB con agregado de C18:2 también muestra bandas adicionales correspondientes a la proteína sensora.
- Fue puesta a punto la solubilización y purificación de la proteína sensora mediante cromatografía de afinidad, lo que finalmente permitió la escisión de bandas individuales para su análisis por MS.
- Los estudios por MS no permitieron identificar proteínas cuya masa corresponda con la diferencia de tamaño observada entre las bandas que reaccionan con anticuerpos anti-PhoQ, ni péptidos con masa diferencial que correspondan a PTMs de la proteína PhoQ.
- Se logró monitorear la cisteína (Cys) 395 en las muestras, concluyéndose que la misma no se encuentra modificada previamente a la corrida electroforética. No se pudo realizar el mismo análisis sobre la Cys-392, ya que en ninguna de las muestras se detectaron péptidos que la contengan.
- Estudios con variantes quimeras entre PhoQ y EnvZ o con versiones truncas de la proteína PhoQ, permiten sugerir que la PTMs ocurriría en el extremo C-terminal citoplásmico, y que es necesario el anclaje de la proteína a la membrana interna para que esta modificación se lleve a cabo.
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