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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., 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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0011-55FE-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CF06-D
Genre: Journal Article

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 Creators:
Golas, M. M.1, Author              
Sander, B.1, Author              
Bessonov, S.2, Author              
Grote, M., Author
Wolf, E., Author
Kastner, B.2, Author              
Stark, H.1, Author              
Lührmann, R.2, Author              
Affiliations:
1Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578577              
2Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              

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 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.

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Language(s): eng - English
 Dates: 2010-12-212010-12-22
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2010.11.023
 Degree: -

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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 40 (6) Sequence Number: - Start / End Page: 927 - 938 Identifier: ISSN: 1097-2765