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Mol Cell. 2001 Feb;7(2):319-29.

A biochemical function for the Sm complex.

Author information

1
Howard Hughes Medical Institute, Department of Biology, Brandeis University, Waltham, MA 02254, USA.

Abstract

Within the yeast commitment complex, SmB, SmD1, and SmD3 make direct contact with the pre-mRNA substrate, close to the 5' splice site. Only these three Sm proteins have long and highly charged C-terminal tails, in metazoa as well as in yeast. We replaced these proteins with tail-truncated versions. Genetic assays demonstrate that the tails contribute to similar and overlapping functions, and cross-linking assays show that the tails make direct contact with the pre-mRNA in a largely sequence-independent manner. Other biochemical assays indicate that they function at least in part to stabilize the U1 snRNP-pre-mRNA interaction. We speculate that this role may be general, and may have even evolved to aid weak intermolecular nucleic acid interactions of only a few base pairs.

PMID:
11239461
DOI:
10.1016/s1097-2765(01)00180-0
[Indexed for MEDLINE]
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