Note. The novel DNA sequence data for TRAPγ (previously SSRγ) and TRAPδ (previously SSRδ) published here have been deposited with the EMBL sequence databank and are available under the accession numbers RNSSRGAM Z14030 and RNSSRDSUB Z19087, respectively.
A tetrameric complex of membrane proteins in the endoplasmic reticulum
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 214, Issue 2, pages 375–381, June 1993
How to Cite
HARTMANN, E., GÖRLICH, D., KOSTKA, S., OTTO, A., KRAFT, R., KNESPEL, S., BÜRGER, E., RAPOPORT, T. A. and PREHN, S. (1993), A tetrameric complex of membrane proteins in the endoplasmic reticulum. European Journal of Biochemistry, 214: 375–381. doi: 10.1111/j.1432-1033.1993.tb17933.x
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received December 4, 1992) – EJB 92 1738/6
The translocation site (translocon), at which nascent polypeptides pass through the endoplasmic reticulum membrane, contains a component previously called ‘signal sequence receptor’ that is now renamed as ‘translocon-associated protein’ (TRAP). Two glycosylated subunits of the TRAP complex have been identified before (α and β subunits). We now show that the TRAP complex is actually comprised of four membrane proteins (α, β, γ, δ), present in a stoichiometric relation, which are genuine neighbours in intact microsomes. The amino acid sequences of the additional, non-glycosylated subunits were deduced from cloning of the corresponding cDNAs. The δ subunit spans the membrane only once and has its major portion, containing a disulfide bridge, at the lumenal side. The γ subunit is predicted to span the membrane four times.
- TRAM protein
translocating-chain-associating membrane protein
- 151988) Antibodies: a laboratory manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY .& (