A membrane component of the endoplasmic reticulum that may be essential for protein translocation.
AUTOR(ES)
Hartmann, E
RESUMO
We have purified a glycosylated, membrane-spanning protein of relative molecular mass approximately 34,000 (Mr approximately 34 K) from canine microsomes that appears to be essential for protein translocation across the endoplasmic reticulum (ER) as shown by the inhibitory action of antibodies directed against it and of monovalent Fab-fragments produced from them. The ER membrane contains at least as many molecules of the 34 K membrane protein as bound ribosomes. The protein can be detected immunologically in tissues of various organisms, indicating an universal function.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=401152Documentos Relacionados
- Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation.
- Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum.
- LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
- An ATP-binding membrane protein is required for protein translocation across the endoplasmic reticulum membrane.
- The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum.