Conformational rearrangements in the sensory RcsF/OMP complex mediate signal transduction across the bacterial cell envelope.
PLoS Genet
; 19(1): e1010601, 2023 01.
Article
en En
| MEDLINE
| ID: mdl-36706155
ABSTRACT
Timely detection and repair of envelope damage are paramount for bacterial survival. The Regulator of Capsule Synthesis (Rcs) stress response can transduce the stress signals across the multilayered gram-negative cell envelope to regulate gene expression in the cytoplasm. Previous studies defined the overall pathway, which begins with the sensory lipoprotein RcsF interacting with several outer membrane proteins (OMPs). RcsF can also interact with the periplasmic domain of the negative regulator IgaA, derepressing the downstream RcsCDB phosphorelay. However, how the RcsF/IgaA interaction is regulated at the molecular level to activate the signaling in response to stress remains poorly understood. In this study, we used a site-saturated mutant library of rcsF to carry out several independent genetic screens to interrogate the mechanism of signal transduction from RcsF to IgaA. We analyzed several distinct classes of rcsF signaling mutants, and determined the region of RcsF that is critically important for signal transduction. This region is bifunctional as it is important for RcsF interaction with both IgaA and OMPs. The mutant analysis provides strong evidence for conformational changes in the RcsF/OMP complex mediating signal transduction to IgaA, and the first direct evidence that OMPs play an important regulatory role in Rcs signaling.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Proteínas de la Membrana Bacteriana Externa
/
Proteínas de Escherichia coli
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Escherichia coli
Idioma:
En
Revista:
PLoS Genet
Asunto de la revista:
GENETICA
Año:
2023
Tipo del documento:
Article
País de afiliación:
Estados Unidos