ArticleScientific reports2015
Structures of intermediates during RES complex assembly.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Phylogenetic Analysis of Spliceosome SF3a2 in Different Plant Species.International journal of molecular sciences · 2023Article
- An Arabidopsis Retention and Splicing complex regulates root and embryo development through pre-mRNA splicing.Plant physiology · 2022Article
- RES complex is associated with intron definition and required for zebrafish early embryogenesis.PLoS genetics · 2018Article
- Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment.Protein science : a publication of the Protein Society · 2017Article
- Retention and splicing complex (RES) - the importance of cooperativity.RNA biology · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The action of the spliceosome depends on the stepwise cooperative assembly and disassembly of its components. Very strong cooperativity was observed for the RES (Retention and Splicing) hetero-trimeric complex where the affinity from binary to tertiary interactions changes more than 100-fold and affects RNA binding. The RES complex is involved in splicing regulation and retention of not properly spliced pre-mRNA with its three components--Snu17p, Pml1p and Bud13p--giving rise to the two possible intermediate dimeric complexes Pml1p-Snu17p and Bud13p-Snu17p. Here we determined the three-dimensional structure and dynamics of the Pml1p-Snu17p and Bud13p-Snu17p dimers using liquid state NMR. We demonstrate that localized as well as global changes occur along the RES trimer assembly pathway. The stepwise rigidification of the Snu17p structure following the binding of Pml1p and Bud13p provides a basis for the strong cooperative nature of RES complex assembly.
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