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RNA. 2004 Dec;10(12):1855-60. Epub 2004 Nov 3.

RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli.

Author information

1
Max F Perutz Laboratories, Institute of Microbiology and Genetics, Dr. Bohrgasse 9/4, 1030 Vienna, Austria. katharina.semrad@univie.ac.at

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.

PMID:
15525706
PMCID:
PMC1370674
DOI:
10.1261/rna.7121704
[Indexed for MEDLINE]
Free PMC Article

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