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  The RES complex is required for efficient transformation of the precatalytic B spliceosome into an activated Bact complex.

Bao, P., Will, C. L., Urlaub, H., Boon, K. L., & Lührmann, R. (2017). The RES complex is required for efficient transformation of the precatalytic B spliceosome into an activated Bact complex. Genes and Development, 31(23-24), 2416-2429. doi:10.1101/gad.308163.117.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-28D8-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-2E4E-4
Genre: Journal Article

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 Creators:
Bao, P.1, Author              
Will, C. L.1, Author              
Urlaub, H.2, Author              
Boon, K. L.1, Author              
Lührmann, R.1, Author              
Affiliations:
1Department of Cellular Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578576              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Free keywords: Prp2 ATPase/RNA helicase; RES complex; pre-mRNA splicing; spliceosome activation; spliceosome disassembly
 Abstract: The precise function of the trimeric retention and splicing (RES) complex in pre-mRNA splicing remains unclear. Here we dissected the role of RES during the assembly and activation of yeast spliceosomes. The efficiency of pre-mRNA splicing was significantly lower in the absence of the RES protein Snu17, and the recruitment of its binding partners, Pml1 (pre-mRNA leakage protein 1) and Bud13 (bud site selection protein 13), to the spliceosome was either abolished or substantially reduced. RES was not required for the assembly of spliceosomal B complexes, but its absence hindered efficient Bact complex formation. ΔRES spliceosomes were no longer strictly dependent on Prp2 activity for their catalytic activation, suggesting that they are structurally compromised. Addition of Prp2, Spp2, and UTP to affinity-purified ΔRES B or a mixture of B/Bact complexes formed on wild-type pre-mRNA led to their disassembly. However, no substantial disassembly was observed with ΔRES spliceosomes formed on a truncated pre-mRNA that allows Prp2 binding but blocks its activity. Thus, in the absence of RES, Prp2 appears to bind prematurely, leading to the disassembly of the ΔRES B complexes to which it binds. Our data suggest that Prp2 can dismantle B complexes with an aberrant protein composition, suggesting that it may proofread the spliceosome's RNP structure prior to activation.

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Language(s): eng - English
 Dates: 2018-01-122017-12-01
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1101/gad.308163.117
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Title: Genes and Development
Source Genre: Journal
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Pages: - Volume / Issue: 31 (23-24) Sequence Number: - Start / End Page: 2416 - 2429 Identifier: -