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- Title
The RNA helicase Aquarius exhibits structural adaptations mediating its recruitment to spliceosomes.
- Authors
De, Inessa; Bessonov, Sergey; Hofele, Romina; dos Santos, Karine; Will, Cindy L; Urlaub, Henning; Lührmann, Reinhard; Pena, Vladimir
- 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.
- Subjects
RNA helicase; CRYSTAL structure; SPLICEOSOMES; NUCLEOPROTEINS; MESSENGER RNA
- Publication
Nature Structural & Molecular Biology, 2015, Vol 22, Issue 2, p138
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2951