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Journal Article

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

MPS-Authors
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De,  I.
Research Group of Macromolecular Crystallography, MPI for Biophysical Chemistry, Max Planck Society;

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Bessonov,  S.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Hofele,  R.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Will,  C. L.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Lührmann,  R.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Pena,  V.
Research Group of Macromolecular Crystallography, MPI for Biophysical Chemistry, Max Planck Society;

Fulltext (public)

2086402.pdf
(Publisher version), 3MB

Supplementary Material (public)

2086402_Suppl_1.pdf
(Supplementary material), 13MB

2086402_Suppl_2.pdf
(Supplementary material), 2MB

2086402_Suppl_3.pdf
(Supplementary material), 2MB

2086402_Suppl_4.pdf
(Supplementary material), 827KB

2086402_Suppl_5.pdf
(Supplementary material), 821KB

Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-AD2D-5
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.