Stop-transfer efficiency of marginally hydrophobic segments depends on the length of the carboxy-terminal tail.
EMBO Rep
; 4(2): 178-83, 2003 Feb.
Article
em En
| MEDLINE
| ID: mdl-12612608
ABSTRACT
Hydrophobic stop-transfer sequences generally serve to halt the translocation of polypeptide chains across the endoplasmic reticulum membrane and become integrated as transmembrane alpha-helices. Using engineered glycosylation sites as topology reporters, we show that the length of the nascent chain between a hydrophobic segment and the carboxy terminus of the protein can affect stop-transfer efficiency. We also show that glycosylation sites located close to a protein's C terminus are modified in two distinct kinetic phases, one fast and one slow. Our findings suggest that membrane integration of a hydrophobic segment is not simply a question of thermodynamic equilibrium, but can be influenced by details of the translocation mechanism.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Sinais Direcionadores de Proteínas
/
Interações Hidrofóbicas e Hidrofílicas
Idioma:
En
Revista:
EMBO Rep
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Suécia