Periplasmic accumulation of truncated forms of outer-membrane PhoE protein of Escherichia coli K-12.
J Mol Biol
; 189(3): 449-55, 1986 Jun 05.
Article
en En
| MEDLINE
| ID: mdl-3537309
ABSTRACT
In order to localize the information within PhoE protein of Escherichia coli K-12 required for export of the protein to the outer membrane, we have generated deletions throughout the phoE gene. Immunocytochemical labelling on ultrathin cryosections revealed that the polypeptides encoded by the mutant alleles are transported to, and accumulate in, the periplasm. These results show that, except for the signal sequence, there is no specific sequence within the PhoE protein that is essential for transport through the cytoplasmic membrane. The overall structure of the protein, rather than a particular sequence of amino acids, seems to be important for assembly into the outer membrane.
Buscar en Google
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas de la Membrana Bacteriana Externa
/
Escherichia coli
Idioma:
En
Revista:
J Mol Biol
Año:
1986
Tipo del documento:
Article