TY - JOUR
T1 - A tetrameric complex of membrane proteins in the endoplasmic reticulum
AU - HARTMANN, Enno
AU - GÖRLICH, Dirk
AU - KOSTKA, Susanne
AU - OTTO, Albrecht
AU - KRAFT, Regine
AU - KNESPEL, Signe
AU - BÜRGER, Elke
AU - RAPOPORT, Tom A.
AU - PREHN, Siegfried
PY - 1993/1/1
Y1 - 1993/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0027285765&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1993.tb17933.x
DO - 10.1111/j.1432-1033.1993.tb17933.x
M3 - Journal articles
C2 - 7916687
AN - SCOPUS:0027285765
SN - 0014-2956
VL - 214
SP - 375
EP - 381
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 2
ER -