RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli

  1. KATHARINA SEMRAD1,
  2. RACHEL GREEN2, and
  3. RENÉE SCHROEDER1
  1. 1Max Perutz Laboratories, Institute of Microbiology and Genetics, 1030 Vienna, Austria
  2. 2Institute of Molecular Biology, Johns Hopkins University, Baltimore, Maryland 21205, USA

Abstract

The ribosome is a highly dynamic ribonucleoprotein machine. During assembly and during translation the ribosomal RNAs must routinely be prevented from falling into kinetic folding traps. Stable occupation of these trapped states may be prevented by proteins with RNA chaperone activity. Here, ribosomal proteins from the large (50S) ribosome subunit of Escherichia coli were tested for RNA chaperone activity in an in vitro trans splicing assay. Nearly a third of the 34 large ribosomal subunit proteins displayed RNA chaperone activity. We discuss a possible role of this function during ribosome assembly and during translation.

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  1. Published in Advance November 3, 2004, doi: 10.1261/rna.7121704 RNA 10: 1855-1860 Copyright 2004 by RNA Society

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