Bacillus subtilis Ffh, a homologue of mammalian SRP54, can intrinsically bind to the precursors of secretory proteins.
Biochem Biophys Res Commun
; 227(3): 762-7, 1996 Oct 23.
Article
en En
| MEDLINE
| ID: mdl-8886007
We analyzed the binding activity of B. subtilis Ffh to the precursors of secretory proteins by purifying mature and precursor proteins of beta-lactamase derived from pUC18 and its derivatives, of which the signal peptide region was replaced with that of E. coli OmpA, B. subtilis AprE, PBP5* or an alkalophilic Bacillus sp. #1011 CGTase. Each of them was mixed with purified B. subtilis Ffh in the presence of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDAC). The tested precursor proteins, including those of E. coli, of which the signal sequences differ from those of B. subtilis in the number of charged amino acids and hydrophobicity, cross-linked with Ffh, whereas mature proteins did not. The addition of scRNA, the B. subtilis counterpart of mammalian SRP 7S RNA, into the mixture did not affect the complex formation. These findings suggest that B. subtilis Ffh intrinsically binds to several precursor proteins.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Precursores de Proteínas
/
Bacillus subtilis
/
Proteínas Bacterianas
/
Partícula de Reconocimiento de Señal
/
Proteínas de Escherichia coli
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1996
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Estados Unidos