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Formation of SRP-like particle induces a conformational change in E. coli 4.5S RNA

Lentzen, Georg ; Dobberstein, Bernhard ; Wintermeyer, Wolfgang

In: FEBS Letters, 348 (1994), pp. 233-238

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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.

Item Type: Article
Journal or Publication Title: FEBS Letters
Volume: 348
Date Deposited: 10 Apr 2008 11:25
Date: 1994
Page Range: pp. 233-238
Faculties / Institutes: Service facilities > Center for Molecular Biology Heidelberg
Subjects: 570 Life sciences
Schriftenreihe ID: Works by Bernhard Dobberstein
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