Molecular architecture of the Saccharomyces cerevisiae activated spliceosome
2016 | journal article. A publication with affiliation to the University of Göttingen.
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Molecular architecture of the Saccharomyces cerevisiae activated spliceosome
Rauhut, R.; Fabrizio, P.; Dybkov, O.; Hartmuth, K.; Pena, V.; Chari, A. & Kumar, V. et al. (2016)
Science, 353(6306) pp. 1399-1405. DOI: https://doi.org/10.1126/science.aag1906
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Details
- Authors
- Rauhut, Reinhard; Fabrizio, Patrizia; Dybkov, Olexandr; Hartmuth, Klaus; Pena, Vladimir; Chari, Ashwin; Kumar, Vinay; Lee, Chung-Tien ; Urlaub, Henning ; Kastner, Berthold; Stark, Holger ; Lührmann, Reinhard
- Abstract
- The activated spliceosome (B-act) is in a catalytically inactive state and is remodeled into a catalytically active machine by the RNA helicase Prp2, but the mechanism is unclear. Here, we describe a 3D electron cryomicroscopy structure of the Saccharomyces cerevisiae B-act complex at 5.8-angstrom resolution. Our model reveals that in B-act, the catalytic U2/U6 RNA-Prp8 ribonucleoprotein core is already established, and the 5' splice site (ss) is oriented for step 1 catalysis but occluded by protein. The first-step nucleophile-the branchsite adenosine-is sequestered within the Hsh155 HEAT domain and is held 50 angstroms away from the 5' ss. Our structure suggests that Prp2 adenosine triphosphatase-mediated remodeling leads to conformational changes in Hsh155's HEAT domain that liberate the first-step reactants for catalysis.
- Issue Date
- 2016
- Status
- published
- Publisher
- Amer Assoc Advancement Science
- Journal
- Science
- ISSN
- 1095-9203; 0036-8075
- Sponsor
- Deutsche Forschungsgemeinschaft [SFB 860]