eprintid: 8577
rev_number: 12
eprint_status: archive
userid: 1
dir: disk0/00/00/85/77
datestamp: 2008-07-22 14:49:05
lastmod: 2016-01-11 14:29:00
status_changed: 2012-08-14 15:25:57
type: article
metadata_visibility: show
creators_name: Lipp, Joachim
creators_name: Dobberstein, Bernhard
creators_name: Haeuptle, Marie-Theres
title: Signal Recognition Particle Arrests Elongation of Nascent Secretory and Membrane Proteins at Multiple Sites in a Transient Manner
ispublished: pub
subjects: 570
divisions: 706000
abstract: The signal recognition particle (SRP) has been shown to target nascent secretory and membrane proteins to the endoplasmic reticulum. In the wheat germ cell-free system, SRP arrests the elongation of the nascent chains until the translational complex is docked to the endoplasmic reticulum membrane where the interaction between SRP and docking protein causes a release of the nascent chain arrest. For two secretory proteins, arrested peptides of 70 amino acids have been identified (Walter, P., Ibrahimi, I., and Blobel, G. (1981) J. Cell Biol. 91, 545-550; Meyer, D. I., Krause, E., and Dobberstein, B. (1982) Nature 297, 647-650). By using an in vitro coupled transcriptiontranslation system, we have analyzed SRP arrest and the resulting peptides of the two secretory proteins lysozyme and granulocyte-macrophage colony-stimulating factor and the membrane protein invariant chain. SRP arrested the elongation of all three proteins at multiple sites, giving rise to ladders of arrested peptides. The size of the arrested peptides increased with the time of translation, resulting in mostly fulllength pre-peptides after about 40 min. This suggests that SRP arrest is transient rather than stable. Upon addition of microsomes, the SRP arrest was released, and all the blocked peptides could be chased into maturf proteins or full-length precursors.
abstract_translated_lang: eng
date: 1987
date_type: published
id_scheme: DOI
id_number: 10.11588/heidok.00008577
schriftenreihe_cluster_id: sr-2
schriftenreihe_order: 038
ppn_swb: 1354705017
own_urn: urn:nbn:de:bsz:16-opus-85773
language: eng
bibsort: LIPPJOACHISIGNALRECO1987
full_text_status: public
publication: The Journal of Biological Chemistry
volume: 262
number: 4
pagerange: 1680-1684
citation:   Lipp, Joachim ; Dobberstein, Bernhard ; Haeuptle, Marie-Theres  (1987) Signal Recognition Particle Arrests Elongation of Nascent Secretory and Membrane Proteins at Multiple Sites in a Transient Manner.  The Journal of Biological Chemistry, 262 (4).  pp. 1680-1684.      
document_url: https://archiv.ub.uni-heidelberg.de/volltextserver/8577/1/Lipp_1987_JBC.pdf