eprintid: 8476
rev_number: 16
eprint_status: archive
userid: 1
dir: disk0/00/00/84/76
datestamp: 2008-06-17 17:36:20
lastmod: 2015-12-31 11:47:11
status_changed: 2012-08-14 15:25:37
type: article
metadata_visibility: show
creators_name: Görlich, Dirk
creators_name: Prehn, Siegfried
creators_name: Hartmann, Enno
creators_name: Herz, Joachim
creators_name: Otto, Albrecht
creators_name: Kraft, Regine
creators_name: Wiedmann, Martin
creators_name: Knespel, Siegne
creators_name: Dobberstein, Bernhard
creators_name: Rapoport, Tom A.
title: The Signal Sequence Receptor Has a Second Subunit and IsPart of a Translocation Complex in the Endoplasmic Reticulum as Probed by Bifunctional Reagents
ispublished: pub
subjects: ddc-570
divisions: i-706000
abstract: Bifunctional cross-linking reagents were used to probe the protein environment in the ER membrane of the signal sequence receptor (SSR), a 34-kD integral membrane glycoprotein (Wiedmann, M., T. V. Kurzchalia, E. Hartmarm, and T. A. Rapoport. 1987. Nature [Lond.]. 328:830-833). The proximity of several polypeptides was demonstrated. A 22-kD glycoprotein was identified tightly bound to the 34-kD SSR even after membrane solubilization. The 34-kD polypeptide, now termed otSSR, and the 22-kD polypeptide, the #SSR, represent a heterodimer. We report on the sequence of the/3SSR, its membrane topology, and on the mechanism of its integration into the membrane. Cross-linking also produced dimers of the a-subunit of the SSR indicating that oligomers of the SSR exist in the ER membrane. Various bifunctional cross-linking reagents were used to study the relation to ER membrane proteins of nascent chains of preprolactin and/3-1actamase at different stages of their translocation through the membrane. The predominant cross-linked products obtained in high yields contained the aSSR, indicating in conjunction with previous results that it is a major membrane protein in the neighborhood of translocating nascent chains of secretory proteins. The results support the existence of a translocon, a translocation complex involving the SSR, which constitutes the specific site of protein translocation across the ER membrane.
abstract_translated_lang: eng
date: 1990
date_type: published
id_scheme: DOI
id_number: 10.11588/heidok.00008476
schriftenreihe_cluster_id: sr-2
schriftenreihe_order: 049
ppn_swb: 135258638X
own_urn: urn:nbn:de:bsz:16-opus-84764
language: eng
bibsort: GORLICHDIRTHESIGNALS1990
full_text_status: public
publication: The Journal of Cell Biology
volume: 111
number: 6
pagerange: 2283-2294
citation:   Görlich, Dirk ; Prehn, Siegfried ; Hartmann, Enno ; Herz, Joachim ; Otto, Albrecht ; Kraft, Regine ; Wiedmann, Martin ; Knespel, Siegne ; Dobberstein, Bernhard ; Rapoport, Tom A.  (1990) The Signal Sequence Receptor Has a Second Subunit and IsPart of a Translocation Complex in the Endoplasmic Reticulum as Probed by Bifunctional Reagents.  The Journal of Cell Biology, 111 (6).  pp. 2283-2294.      
document_url: https://archiv.ub.uni-heidelberg.de/volltextserver/8476/1/Goerlich_1990_JCB.pdf