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. 1990 Feb 15;266(1):149–156. doi: 10.1042/bj2660149

Interactions of signal peptides with signal-recognition particle.

A Robinson 1, O M Westwood 1, B M Austen 1
PMCID: PMC1131108  PMID: 2155605

Abstract

The mechanisms whereby isolated or synthetic signal peptides inhibit processing of newly synthesized prolactin in microsome-supplemented lysates from reticulocytes and wheat-germ were investigated. At a concentration of 5 microM, a consensus signal peptide reverses the elongation arrest imposed by the signal-recognition particle (SRP), and at higher concentrations in addition inhibits elongation of both secretory and non-secretory proteins. A photoreactive form of a synthetic signal peptide cross-links under u.v. illumination to the 54 kDa and 68 kDa subunits of SRP, whereas the major cross-linked protein produced after photoreaction of rough microsomes is of 45 kDa. As SRP-mediated elongation arrest is unlikely to be essential for translocation, it is suggested that signal peptides may interact with components other than SRP in the translation system in vitro.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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