Nucleic Acids Research, Vol 25, Issue 6 1117-1122, Copyright © 1997 by Oxford University Press
DY Chang, JA Newitt, K Hsu, HD Bernstein and RJ Maraia
Binding of the signal recognition particle (SRP) to signal sequences during
translation leads to an inhibition of polypeptide elongation known as
translation arrest. The arrest activity is mediated by a discrete domain
comprised of the Alu portion of SRP RNA and a 9 and 14 kDa polypeptide
heterodimer (SRP9/14). Although very few nucleotides in SRP RNA are
conserved throughout evolution, the remarkable conservation of G24, which
resides in the region of SRP9/14 interaction, suggests that it is essential
for translation arrest. To understand the functional significance of the
G24 residue, we made single base substitutions in SRP RNA at this position
and analyzed the ability of the mutants to bind SRP9/14 and to reconstitute
functional SRPs. Mutation of G24 to C reduced binding to SRP9/14 by at
least 50-fold, whereas mutation to A and U reduced binding approximately 2-
and 5-fold respectively. The mutant RNAs could nevertheless assemble into
SRPs at high subunit concentrations. SRPs reconstituted with mutant RNAs
were not significantly defective in translation arrest assays, indicating
that the conserved guanosine does not interact directly with the
translational machinery. Taken together, these results demonstrate that G24
plays an important role in the translation arrest function of SRP by
mediating high affinity binding of SRP9/14.
ARTICLES
A highly conserved nucleotide in the Alu domain of SRP RNA mediates translation arrest through high affinity binding to SRP9/14
Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
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