Nucleic Acids Research, Vol 27, Issue 2 587-595, Copyright © 1999 by Oxford University Press
RL Seipelt, B Zheng, A Asuru and BC Rymond
Core snRNP proteins bind snRNA through the conserved Sm site,
PuA(U)n>/=3GPu. While yeast U1 snRNA has three matches to the Sm
consensus, the U1 3'-terminal Sm site was found to be both necessary and
sufficient for U1 function. Mutation of this site inhibited pre- mRNA
splicing, blocked cell division and resulted in the accumulation of two
3'-extended forms of the U1 snRNA. Cells which harbor the Sm site mutation
lack mature U1 RNA (U1alpha) but have a minor polyadenylated species,
U1gamma, and a prominent, non-polyadenylated species, U1beta. Metabolic
depletion of the essential Sm core protein, Smd1p, also resulted in the
increased accumulation of U1beta and U1gamma. In vitro, synthetic U1
precursors were cleaved by Rnt1p (RNase III) very near the U1beta 3'-end
observed in vivo. We propose that U1beta is an Rnt1p-cleaved intermediate
and that U1 maturation to the U1alpha form occurs through an Sm-sensitive
step. Interestingly, both U1alpha and a second, much longer RNA,
U1straightepsilon, were produced in an rnt1 mutant strain. These results
suggest that yeast U1 snRNA processing may progress through Rnt1p-dependent
and Rnt1p-independent pathways, both of which require a fun-ctional Sm site
for final snRNA maturation.
ARTICLES
U1 snRNA is cleaved by RNase III and processed through an Sm site- dependent pathway
T. H. Morgan School of Biological Sciences and the Markey Cancer Center, University of Kentucky, Lexington,KY 40506-0225, USA.
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