Abstract
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.
| Original language | English |
|---|---|
| Journal | European Journal of Biochemistry |
| Volume | 214 |
| Issue number | 2 |
| Pages (from-to) | 375-381 |
| Number of pages | 7 |
| ISSN | 0014-2956 |
| DOIs | |
| Publication status | Published - 01.01.1993 |
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