Nucleic Acids Research, Vol 25, Issue 9 1788-1794, Copyright © 1997 by Oxford University Press
S Abou Elela and RN Nazar
Studies on the inhibition of protein synthesis by specific anti 5.8S rRNA
oligonucleotides have suggested that this RNA plays an important role in
eukaryotic ribosome function. Mutations in the 5. 8S rRNA can inhibit cell
growth and compromise protein synthesis in vitro . Polyribosomes from cells
expressing these mutant 5.8S rRNAs are elevated in size and
ribosome-associated tRNA. Cell free extracts from these cells also are more
sensitive to antibiotics which act on the 60S ribosomal subunit by
inhibiting elongation. The extracts are especially sensitive to
cycloheximide and diphtheria toxin which act specifically to inhibit
translocation. Studies of ribosomal proteins show no reproducible changes
in the core proteins, but reveal reduced levels of elongation factors 1 and
2 only in ribosomes which contain large amounts of mutant 5.8S rRNA.
Polyribosomes from cells which are severely inhibited, but contain little
mutant 5.8S rRNA, do not show the same reductions in the elongation
factors, an observation which underlines the specific nature of the change.
Taken together the results demonstrate a defined and critical function for
the 5.8S rRNA, suggesting that this RNA plays a role in ribosome
translocation.
ARTICLES
Role of the 5.8S rRNA in ribosome translocation
Department of Molecular Biology and Genetics, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
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