Reference: Zhang D, et al. (2001) A biochemical function for the Sm complex. Mol Cell 7(2):319-29

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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.

Reference Type
Journal Article
Authors
Zhang D, Abovich N, Rosbash M
Primary Lit For
SMD1 | SMB1 | SMD3 | U1 small nuclear ribonucleoprotein complex