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Structures of intermediates during RES complex assembly.

<div class='caption-title'>Three-dimensional structures of intermediates during cRES complex assembly.</div>
<div class='caption-title'>Comparison of the 3D structures of the RES core complex, the cPml1p–cSnu17p dimer and the hcBud13p–cSnu17p dimer.</div>
<div class='caption-title'>Analysis of HN RDCs observed in cSnu17p when part of the cPml1p–cSnu17p dimer, the hcBud13p–cSnu17p dimer and cRES.</div>
Wysoczanski P, Becker S, Zweckstetter M
OpenAccess logo Sci Rep 5 12545 (2015)
Cited: 5 times
EuropePMC logo PMID: 26212312

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.

Articles citing this publication (5)

  1. RES complex is associated with intron definition and required for zebrafish early embryogenesis. Fernandez JP, Moreno-Mateos MA, Gohr A, Miao L, Chan SH, Irimia M, Giraldez AJ. PLoS Genet 14 e1007473 (2018)
  2. Retention and splicing complex (RES) - the importance of cooperativity. Wysoczanski P, Zweckstetter M. RNA Biol 13 128-133 (2016)
  3. Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment. Kuwasako K, Nameki N, Tsuda K, Takahashi M, Sato A, Tochio N, Inoue M, Terada T, Kigawa T, Kobayashi N, Shirouzu M, Ito T, Sakamoto T, Wakamatsu K, Güntert P, Takahashi S, Yokoyama S, Muto Y. Protein Sci 26 280-291 (2017)
  4. An Arabidopsis Retention and Splicing complex regulates root and embryo development through pre-mRNA splicing. Xiong F, Xiong F, Ren JJ, Wang YY, Zhou Z, Qi HD, Otegui MS, Wang XL. Plant Physiol 190 621-639 (2022)
  5. Phylogenetic Analysis of Spliceosome SF3a2 in Different Plant Species. Tian Y, Das D, Li M, Song T, Yang J, Liu Y. Int J Mol Sci 24 5232 (2023)


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