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The Signal Sequence Interacts with the Methionine-rich Domain of the 54-kD Protein of Signal Recognition Particle

High, Stephen ; Dobberstein, Bernhard

In: The Journal of Cell Biology , 113 (1991), Nr. 2. pp. 223-233

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The signal sequence of nascent preprolactin interacts with the 54-kD protein of the signal recognition particle (SRP54). To identify the domain or site on SRP54 that interacts with the signal sequence we used a photocross-linking approach followed by limited proteolysis and immunoprecipitation using anti-peptide antibodies specific for defined regions of SRP54. We found that the previously identified methionine-rich RNA-binding domain of SRP54 (SRP54M domain) also interacts with the signal sequence. The smallest fragment that was found to be crosslinked to the signal sequence comprised the COOH-terminal 6-kD segment of the SRP54M domain. No cross-link to the putative GTP-binding domain of SRP54 (SRP54G domain) was found. Proteolytic cleavage between the SRP54M domain and SRP54G domain did not impair the subsequent interaction between the signal sequence and the SRP54M domain. Our results show that both the RNA binding and signal sequence binding functions of SRP54 are performed by the SRP54M domain.

Item Type: Article
Journal or Publication Title: The Journal of Cell Biology
Volume: 113
Number: 2
Date Deposited: 17 Jul 2008 17:11
Date: 1991
Page Range: pp. 223-233
Faculties / Institutes: Service facilities > Center for Molecular Biology Heidelberg
Subjects: 570 Life sciences
Schriftenreihe ID: Works by Bernhard Dobberstein
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