Nucleic Acids Research, Vol 27, Issue 4 1025-1031, Copyright © 1999 by Oxford University Press
Q Huang and T Pederson
The biosynthesis of U1, U2, U4 and U5 spliceosomal small nuclear RNAs
(snRNAs) involves the nuclear export of precursor molecules extended at
their 3' ends, followed by a cytoplasmic phase during which the pre- snRNAs
assemble into ribonucleoprotein particles and undergo hypermethylation of
their 5' caps and 3' end processing prior to nuclear import. Previous
studies have demonstrated that the assembly of pre-snRNAs into
ribonucleoprotein particles containing the Sm core proteins is essential
for nuclear import in mammalian cells but that 5' cap hypermethylation is
not. In the present investigation we have asked whether or not 3' end
processing is required for nuclear import of U2 RNA. We designed human
pre-U2 RNAs that carried modified 3' tails, and identified one that was
stalled (or greatly slowed) in 3' end processing, leading to its
accumulation in the cytoplasm of human cells. Nonetheless, this 3'
processing arrested pre-U2 RNA molecule was found to undergo cytoplasmic
assembly into Sm protein-containing complexes to the same extent as normal
pre-U2 RNA. The Sm protein- associated, unprocessed mutant pre-U2 RNA was
not observed in the nuclear fraction. Using an assay based on suppression
of a genetically blocked SV40 pre-mRNA splicing pathway, we found that the
3' processing deficient U2 RNA was significantly reduced in its ability to
rescue splicing, consistent with its impaired nuclear import.
ARTICLES
A human U2 RNA mutant stalled in 3' end processing is impaired in nuclear import
Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, 377 Plantation Street, Worcester, MA 01605, USA.
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