Anti-(p34 protein) antibodies inhibit ribosome binding to and protein translocation across the rough microsomal membrane.
FEBS Lett
; 326(1-3): 241-5, 1993 Jul 12.
Article
em En
| MEDLINE
| ID: mdl-8325372
ABSTRACT
The p34 protein is a non-glycosylated, integral membrane protein characteristic of rough microsomes and is believed to play a role in the ribosome-membrane association. Here, antibodies directed against p34 were examined as to their inhibitory effect on ribosome binding to and protein translocation across the microsomal membrane. Preincubation of the stripped (ribosome-depleted) membrane with anti-p34 immunoglobulins (IgGs) or their Fab fragments led to more than 80% inhibition of the binding of ribosomes and their large (60S) subunit to the membrane. The inhibition was dependent on the amount of antibodies used, but comparable amounts of IgGs and Fab fragments from nonimmune serum had less effect. The p34 antibodies were also inhibitory for cotranslational translocation of secretory proteins, i.e. placental lactogen and serum albumin, across the membrane. These results suggest that p34 is involved in the binding of ribosomes to the microsomal membrane and that it is in close proximity to the protein translocation site in the microsomal membrane.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ribossomos
/
Membranas Intracelulares
/
Proteínas de Membrana
/
Microssomos
/
Anticorpos
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1993
Tipo de documento:
Article
País de afiliação:
Japão