The ribosomal translocase homologue Snu114p is involved in unwinding U4/U6 RNA during activation of the spliceosome.

ABSTRACT: Snu114p is a yeast U5 snRNP protein homologous to the ribosomal elongation factor EF-2. Snu114p exhibits the same domain structure as EF-2, including the G-domain, but with an additional N-terminal domain. To test whether Snu114p in the spliceosome is involved in rearranging RNA secondary structures (by analogy to EF-2 in the ribosome), we created conditionally lethal mutants. Deletion of this N-terminal domain (snu114 Delta N) leads to a temperature-sensitive phenotype at 37 degrees C and a pre-mRNA splicing defect in vivo. Heat treatment of snu114 Delta N extracts blocked splicing in vitro before the first step. The snu114 Delta N still associates with the tri-snRNP, and the stability of this particle is not significantly impaired by thermal inactivation. Heat treatment of snu114 Delta N

SUBMITTER: Bartels C 

PROVIDER: S-EPMC1084225 | biostudies-literature | 2002 Sep

REPOSITORIES: biostudies-literature