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Molecular architecture of the Saccharomyces cerevisiae activated spliceosome.

MPG-Autoren
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Rauhut,  R.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Fabrizio,  P.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Dybkov,  O.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Hartmuth,  K.
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;

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Chari,  A.
Research Group of Structural Biochemistry and Mechanisms, MPI for Biophysical Chemistry, Max Planck Society;

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Kumar,  V.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Lee,  C. T.
Research Group of Bioanalytical Mass Spectrometry, 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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Kastner,  B.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Stark,  H.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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

Externe Ressourcen

http://www.sciencemag.org/cgi/pmidlookup?view=long&pmid=27562955
(Verlagsversion)

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Ergänzendes Material (frei zugänglich)

2332520-Suppl-1.pdf
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2332520-Suppl-3.mov
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aag1906s1.mp4
(Ergänzendes Material), 405KB

Zitation

Rauhut, R., Fabrizio, P., Dybkov, O., Hartmuth, K., Pena, V., Chari, A., et al. (2016). Molecular architecture of the Saccharomyces cerevisiae activated spliceosome. Science, 353(6306), 1399-1405. doi:10.1126/science.aag1906.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002B-3346-F
Zusammenfassung
The activated spliceosome (Bact) 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 S. cerevisiae Bact complex at 5.8 Å resolution. Our model reveals that in Bact 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 Å away from the 5'ss. Our structure suggests that Prp2 ATPase-mediated remodeling leads to conformational changes in Hsh155's HEAT domain that liberate the first step reactants for catalysis.