eprintid: 8593
rev_number: 22
eprint_status: archive
userid: 1
dir: disk0/00/00/85/93
datestamp: 2009-03-02 11:00:33
lastmod: 2016-01-15 07:34:46
status_changed: 2012-08-14 15:28:11
type: article
metadata_visibility: show
creators_name: Scoulica, Efstathia
creators_name: Krause, Elke
creators_name: Meese, Klaus
creators_name: Dobberstein, Bernhard
title: Disassembly and domain structure of the proteins in the signal-recognition particle
ispublished: pub
subjects: ddc-570
divisions: i-706000
abstract: The signal-recognition particle (SRP) is a ribonucleoprotein (RNP) complex consisting of six different polypeptide chains and a 7SL RNA. It participates in initiating the translocation of proteins across the membrane of the endoplasmic reticulum, SRP was disassembled in 2 M KCl into three components, one RNP composed of 7SL RNA and the 54-kDa and 19-kDa proteins, and two heterodimers consisting of the 72/68-kDa and the 14/9-kDa proteins respectively. The 54-kDa protein could be released from the RNP subparticle by chromatography on DEAE-Sepharose in Mg2 ’ -depleted buffer, while the 19-kDa protein remained bound to the 7SL RNA. The domain structure of SRP proteins was probed by using mild elastase treatment and protein-specific antibodies. It was found that the 72, 68, 54 and 19-kDa SRP proteins were proteolytically processed in distinct steps. Most remarkably a protein fragment of 55-kDa, generated from the 72-kDa SRP protein, and a 35-kDa fragment from the 54-kDa SRP protein were both released from the RNP particle. Fragments generated from the 68-kDa protein and detectable with the anti-(68-kDa protein) antibody remained associated with the RNP particle. Cleavage of the SRP proteins by elastase at 2.5 pg/ml resulted in partial loss of activity, while 10 lg/ml caused complete inactivation of the particle. Neither the elongation arrest of IgG light chain nor its translocation across SRP-depleted microsomal membranes was promoted. The implications of these results on the possible interaction between the SRP subunits are discussed.
abstract_translated_lang: eng
date: 1987
date_type: published
id_scheme: DOI
id_number: 10.11588/heidok.00008593
schriftenreihe_cluster_id: sr-2
schriftenreihe_order: 039
ppn_swb: 1373877987
own_urn: urn:nbn:de:bsz:16-opus-85935
language: eng
bibsort: SCOULICAEFDISASSEMBL1987
full_text_status: public
publication: European Journal of Biochemistry
volume: 1987
number: 163
pagerange: 519-528
citation:   Scoulica, Efstathia ; Krause, Elke ; Meese, Klaus ; Dobberstein, Bernhard  (1987) Disassembly and domain structure of the proteins in the signal-recognition particle.  European Journal of Biochemistry, 1987 (163).  pp. 519-528.      
document_url: https://archiv.ub.uni-heidelberg.de/volltextserver/8593/1/Scoulica_1987_EJB.pdf