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  The RNA helicase ​Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes.

De, I., Bessonov, S., Hofele, R., Dos Santos, K., Will, C. L., Urlaub, H., et al. (2015). The RNA helicase ​Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes. Nature Structural and Molecular Biology, 22(2), 138-144. doi:10.1038/nsmb.2951.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-AD2D-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-0EAC-B
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 Creators:
De, I.1, Author              
Bessonov, S.2, Author              
Hofele, R.3, Author              
Dos Santos, K., Author
Will, C. L.2, Author              
Urlaub, H.3, Author              
Lührmann, R.2, Author              
Pena, V.1, Author              
Affiliations:
1Research Group of Macromolecular Crystallography, MPI for Biophysical Chemistry, Max Planck Society, ou_2035293              
2Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
3Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: Aquarius is a multifunctional putative RNA helicase that binds precursor-mRNA introns at a defined position. Here we report the crystal structure of human Aquarius, revealing a central RNA helicase core and several unique accessory domains, including an ARM-repeat domain. We show that Aquarius is integrated into spliceosomes as part of a pentameric intron-binding complex (IBC) that, together with the ARM domain, cross-links to U2 snRNP proteins within activated spliceosomes; this suggests that the latter aid in positioning Aquarius on the intron. Aquarius's ARM domain is essential for IBC formation, thus indicating that it has a key protein-protein-scaffolding role. Finally, we provide evidence that Aquarius is required for efficient precursor-mRNA splicing in vitro. Our findings highlight the remarkable structural adaptations of a helicase to achieve position-specific recruitment to a ribonucleoprotein complex and reveal a new building block of the human spliceosome.

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Language(s): eng - English
 Dates: 2015-01-19
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nsmb.2951
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 22 (2) Sequence Number: - Start / End Page: 138 - 144 Identifier: -