eprintid: 8302
rev_number: 8
eprint_status: archive
userid: 1
dir: disk0/00/00/83/02
datestamp: 2008-04-10 11:25:42
lastmod: 2014-08-30 12:06:54
status_changed: 2012-08-14 15:25:07
type: article
metadata_visibility: show
creators_name: Lentzen, Georg
creators_name: Dobberstein, Bernhard
creators_name: Wintermeyer, Wolfgang
title: Formation of SRP-like particle induces a conformational change in E. coli 4.5S RNA
ispublished: pub
subjects: ddc-570
divisions: i-706000
abstract: E. coli P48 protein is homologous to the SRP54 component of the eukaryotic signal recognition particle. In vivo, P48 is associated with 4.5S RNA which shares a homology with eukaryotic SRP RNA. To study the interaction between P48 and 4.5S RNA in vitro, we used 4.5S RNA with fluorescein coupled to the 3'-terminal ribose. Upon binding of P48, the fluorescent 4.5S RNA shows a substantial decrease in fluorescence. Fluorescence quenching as well as anisotropy measurements reveal that the effect is not due to a direct interaction of P48 with the dye. This suggests that the binding of P48 induces a conformational change in 4.5S RNA which affects the structure at the 3' end of the RNA. From equilibrium titrations with fluorescent 4.5S RNA, a dissociation constant of 0.15 microns is obtained for the RNA.protein complex. The formation of the complex is not affected by GTP binding to or hydrolysis by P48.
abstract_translated_lang: eng
date: 1994
date_type: published
id_scheme: DOI
id_number: 10.11588/heidok.00008302
schriftenreihe_cluster_id: sr-2
schriftenreihe_order: 071
ppn_swb: 1349109487
own_urn: urn:nbn:de:bsz:16-opus-83029
language: eng
bibsort: LENTZENGEOFORMATIONO1994
full_text_status: public
publication: FEBS Letters
volume: 348
pagerange: 233-238
citation:   Lentzen, Georg ; Dobberstein, Bernhard ; Wintermeyer, Wolfgang  (1994) Formation of SRP-like particle induces a conformational change in E. coli 4.5S RNA.  FEBS Letters, 348.  pp. 233-238.      
document_url: https://archiv.ub.uni-heidelberg.de/volltextserver/8302/1/Lentzen_1994_FEBSLett.pdf