Nucleic Acids Research, Vol 25, Issue 2 318-326, Copyright © 1997 by Oxford University Press
F Bovia, N Wolff, S Ryser and K Strub
The heterodimeric subunit, SRP9/14, of the signal recognition particle
(SRP) has previously been found to bind to scAlu and scB1 RNAs in vitro and
to exist in large excess over SRP in anthropoid cells. Here we show that
human and mouse SRP9/14 bind with high affinities to other Alu- like RNAs
of different evolutionary ages including the neuron-specific BC200 RNA. The
relative dissociation constants of the different RNA- protein complexes are
inversely proportional to the evolutionary distance between the Alu RNA
species and 7SL RNA. In addition, the human SRP9/14 binds with higher
affinity than mouse SRP9/14 to all RNAs analyzed and this difference is not
explained by the additional C- terminal domain present in the anthropoid
SRP14. The conservation of high affinity interactions between SRP9/14 and
Alu-like RNAs strongly indicates that these Alu-like RNPs exist in vivo and
that they have cellular functions. The observation that human SRP9/14 binds
better than its mouse counterpart to distantly related Alu RNAs, such as
recently transposed elements, suggests that the anthropoid-specific excess
of SRP9/14 may have a role in controlling Alu amplification rather than in
compensating a defect in SRP assembly and functions.
ARTICLES
The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog
Departement de Biologie Cellulaire, Universite de Geneve, Sciences III, CH-1211 Geneva 4, Switzerland.
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