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Journal Article

3D cryo-EM structure of an active step I spliceosome and localization of its catalytic core.

MPS-Authors
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Golas,  M. M.
Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Sander,  B.
Research Group of 3D Electron Cryo-Microscopy, 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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Kastner,  B.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Stark,  H.
Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society;

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

Fulltext (public)

883575.pdf
(Publisher version), 2MB

Supplementary Material (public)

883575-Suppl-1.pdf
(Supplementary material), 512KB

883575-Suppl-2.avi
(Supplementary material), 20MB

883575-Suppl-3.avi
(Supplementary material), 20MB

883575-Suppl-4.avi
(Supplementary material), 20MB

Citation

Golas, M. M., Sander, B., Bessonov, S., Grote, M., Wolf, E., Kastner, B., et al. (2010). 3D cryo-EM structure of an active step I spliceosome and localization of its catalytic core. Molecular Cell, 40(6), 927-938. doi:10.1016/j.molcel.2010.11.023.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0011-55FE-C
Abstract
The spliceosome excises introns from pre-mRNA in a two-step splicing reaction. So far, the three-dimensional (3D) structure of a spliceosome with preserved catalytic activity has remained elusive. Here, we determined the 3D structure of the human, catalytically active step I spliceosome (C complex) by cryo-electron microscopy (cryo-EM) in vitrified ice. Via immunolabeling we mapped the position of the 5′ exon. The C complex contains an unusually salt-stable ribonucleoprotein (RNP) core that harbors its catalytic center. We determined the 3D structure of this RNP core and also that of a post-step II particle, the 35S U5 snRNP, which contains most of the C complex core proteins. As C complex domains could be recognized in these structures, their position in the C complex could be determined, thereby allowing the region harboring the spliceosome's catalytic core to be localized.