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  Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre.

Rasche, N., Dybkov, O., Schmitzova, J., Akyildiz, B., Fabrizio, P., & Lührmann, R. (2012). Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre. EMBO Journal, 31(6), 1591-1604. doi:10.1038/emboj.2011.502.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-8551-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-08C2-B
Genre: Journal Article

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 Creators:
Rasche, N.1, Author              
Dybkov, O.1, Author              
Schmitzova, J.1, Author              
Akyildiz, B., Author
Fabrizio, P.1, Author              
Lührmann, R.1, Author              
Affiliations:
1Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              

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Free keywords: Catalytic centre; Cwc2; RBM22; spliceosome; U6-ISL
 Abstract: RNA-structural elements play key roles in pre-mRNA splicing catalysis; yet, the formation of catalytically com- petent RNA structures requires the assistance of spliceo- somal proteins. We show that the S. cerevisiae Cwc2 protein functions prior to step 1 of splicing, and it is not required for the Prp2-mediated spliceosome remodelling that generates the catalytically active B* complex, suggest- ing that Cwc2 plays a more sophisticated role in the generation of a functional catalytic centre. In active spli- ceosomes, Cwc2 contacts catalytically important RNA ele- ments, including the U6 internal stem-loop (ISL), and regions of U6 and the pre-mRNA intron near the 5 0 splice site, placing Cwc2 at/near the spliceosome’s catalytic centre. These interactions are evolutionarily conserved, as shown by studies with Cwc2’s human counterpart RBM22, indicating that Cwc2/RBM22–RNA contacts are functionally important. We propose that Cwc2 induces an active conformation of the spliceosome’s catalytic RNA elements. Thus, the function of RNA–RNA tertiary inter- actions within group II introns, namely to induce an active conformation of domain V, may be fulfilled by proteins that contact the functionally analogous U6-ISL, within the spliceosome.

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Language(s): eng - English
 Dates: 2012-01-132012-03-21
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/emboj.2011.502
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Title: EMBO Journal
Source Genre: Journal
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Pages: - Volume / Issue: 31 (6) Sequence Number: - Start / End Page: 1591 - 1604 Identifier: -