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. 2010 Apr 5;189(1):11–12. doi: 10.1083/jcb.201002102

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© 2010 Karbstein

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 1. — Models for the function of chaperones in ribosome assembly. (A) Chaperones might prevent the aggregation of the highly charged r-proteins, many of which have unstructured tails, and deliver newly made r-proteins to nascent ribosomes. (B) Chaperones might also act directly upon assembling ribosomes by refolding r-proteins or assembly factors (purple) within preribosomal particles. This is shown as a change from helices to sheets.