Defining the function of OmpA in the Rcs stress response.
Elife
; 92020 09 28.
Article
en En
| MEDLINE
| ID: mdl-32985973
OmpA, a protein commonly found in the outer membrane of Gram-negative bacteria, has served as a paradigm for the study of ß-barrel proteins for several decades. In Escherichia coli, OmpA was previously reported to form complexes with RcsF, a surface-exposed lipoprotein that triggers the Rcs stress response when damage occurs in the outer membrane and the peptidoglycan. How OmpA interacts with RcsF and whether this interaction allows RcsF to reach the surface has remained unclear. Here, we integrated in vivo and in vitro approaches to establish that RcsF interacts with the C-terminal, periplasmic domain of OmpA, not with the N-terminal ß-barrel, thus implying that RcsF does not reach the bacterial surface via OmpA. Our results suggest a novel function for OmpA in the cell envelope: OmpA competes with the inner membrane protein IgaA, the downstream Rcs component, for RcsF binding across the periplasm, thereby regulating the Rcs response.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de la Membrana Bacteriana Externa
/
Transducción de Señal
/
Membrana Celular
/
Proteínas de Escherichia coli
/
Escherichia coli
Idioma:
En
Revista:
Elife
Año:
2020
Tipo del documento:
Article
País de afiliación:
Bélgica
Pais de publicación:
Reino Unido