Nucleic Acids Research, Vol 25, Issue 10 1920-1929, Copyright © 1997 by Oxford University Press
Y Thomas, N Bui and K Strub
The signal recognition particle (SRP) provides the molecular link between
synthesis of polypeptides and their concomitant translocation into the
endoplasmic reticulum. During targeting, SRP arrests or delays elongation
of the nascent chain, thereby presumably ensuring a high translocation
efficiency. Components of the Alu domain, SRP9/14 and the Alu sequences of
SRP RNA, have been suggested to play a role in the elongation arrest
function of SRP. We generated a truncated SRP14 protein, SRP14-20C, which
forms, together with SRP9, a stable complex with SRP RNA. However,
particles reconstituted with SRP9/14-20C, RC(9/14-20C), completely lack
elongation arrest activity. RC(9/14-20C) particles have intact signal
recognition, targeting and ribosome binding activities. SRP9/14-20C
therefore only impairs interactions with the ribosome that are required to
effect elongation arrest. This result provides evidence that direct
interactions between the Alu domain components and the ribosome are
required for this function. Furthermore, SRP9/14-20C binding to SRP RNA
results in tertiary structure changes in the RNA. Our results strongly
indicate that these changes account for the negative effect of SRP14
truncation on elongation arrest, thus revealing a critical role of the RNA
in this function.
ARTICLES
A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle
Departement de Biologie Cellulaire, Universite de Geneve, Sciences III, CH-1211 Geneve 4, Switzerland.
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