The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring.
J Bacteriol
; 187(1): 320-8, 2005 Jan.
Article
en En
| MEDLINE
| ID: mdl-15601716
ABSTRACT
FtsI (also called PBP3) of Escherichia coli is a transpeptidase required for synthesis of peptidoglycan in the division septum and is one of about a dozen division proteins that localize to the septal ring. FtsI comprises a short amino-terminal cytoplasmic domain, a single transmembrane helix (TMH), and a large periplasmic domain that encodes the catalytic (transpeptidase) activity. We show here that a 26-amino-acid fragment of FtsI is sufficient to direct green fluorescent protein to the septal ring in cells depleted of wild-type FtsI. This fragment extends from W22 to V47 and corresponds to the TMH. This is a remarkable finding because it is unusual [corrected] for a TMH to target a protein to a site more specific than the membrane. Alanine-scanning mutagenesis of the TMH identified several residues important for septal localization. These residues cluster on one side of an alpha-helix, which we propose interacts directly with another division protein to recruit FtsI to the septal ring.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Estructura Secundaria de Proteína
/
Proteínas de Escherichia coli
/
Proteínas de Unión a las Penicilinas
/
Peptidoglicano Glicosiltransferasa
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
J Bacteriol
Año:
2005
Tipo del documento:
Article
País de afiliación:
Estados Unidos