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  A tetrameric complex of membrane proteins in the endoplasmic reticulum.

Hartmann, E., Görlich, D., Kostka, S., Otto, A., Kraft, R., Knespel, S., et al. (1993). A tetrameric complex of membrane proteins in the endoplasmic reticulum. European Journal of Biochemistry, 214(2), 375-381. doi:10.1111/j.1432-1033.1993.tb17933.x.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-3BD2-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C506-1
Genre: Journal Article

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1922630.pdf (Publisher version), 885KB
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 Creators:
Hartmann, E., Author
Görlich, D.1, Author              
Kostka, S., Author
Otto, A., Author
Kraft, R., Author
Knespel, S., Author
Bürger, E., Author
Rapoport, T. A., Author
Prehn, S., Author
Affiliations:
1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              

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 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.

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Language(s): eng - English
 Dates: 2005-03-031993-06
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: European Journal of Biochemistry
Source Genre: Journal
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Pages: - Volume / Issue: 214 (2) Sequence Number: - Start / End Page: 375 - 381 Identifier: -