Send to

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

A biochemical function for the Sm complex.

Author information

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


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.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center