3D Cryo-EM Structure of an Active Step I Spliceosome and Localization of Its Catalytic Core
2010 | journal article. A publication with affiliation to the University of Göttingen.
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3D Cryo-EM Structure of an Active Step I Spliceosome and Localization of Its Catalytic Core
Golas, M. M.; Sander, B.; Bessonov, S.; Grote, M.; Wolf, E.; Kastner, B. & Stark, H. et al. (2010)
Molecular Cell, 40(6) pp. 927-938. DOI: https://doi.org/10.1016/j.molcel.2010.11.023
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Details
- Authors
- Golas, Mariola Monika; Sander, Bjoern; Bessonov, Sergey; Grote, Michael; Wolf, Elmar; Kastner, Berthold; Stark, Holger ; Lührmann, Reinhard
- 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.
- Issue Date
- 2010
- Status
- published
- Publisher
- Cell Press
- Journal
- Molecular Cell
- ISSN
- 1097-2765