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  Cryo-EM structure of a pre-catalytic human spliceosome primed for activation.

Bertram, K., Agafonov, D. E., Dybkov, O., Haselbach, D., Leelaram, M. N., Will, C. L., et al. (2017). Cryo-EM structure of a pre-catalytic human spliceosome primed for activation. Cell, 170(4), 701-713, e1 - e4. doi:10.1016/j.cell.2017.07.011.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-B9FC-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-9B1C-1
Genre: Journal Article

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 Creators:
Bertram, K.1, Author              
Agafonov, D. E.2, Author              
Dybkov, O.2, Author              
Haselbach, D.1, Author              
Leelaram, M. N.2, Author              
Will, C. L.2, Author              
Urlaub, H.3, Author              
Kastner, B.2, Author              
Lührmann, R.2, Author              
Stark, H.1, Author              
Affiliations:
1Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              
2Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
3Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Free keywords: B complex spliceosome; B-specific proteins; cryo-EM; pre-catalytic spliceosome; pre-mRNA splicing; spliceosome; spliceosome structure
 Abstract: Little is known about the spliceosome's structure before its extensive remodeling into a catalytically active complex. Here, we report a 3D cryo-EM structure of a pre-catalytic human spliceosomal B complex. The U2 snRNP-containing head domain is connected to the B complex main body via three main bridges. U4/U6.U5 tri-snRNP proteins, which are located in the main body, undergo significant rearrangements during tri-snRNP integration into the B complex. These include formation of a partially closed Prp8 conformation that creates, together with Dim1, a 5' splice site (ss) binding pocket, displacement of Sad1, and rearrangement of Brr2 such that it contacts its U4/U6 substrate and is poised for the subsequent spliceosome activation step. The molecular organization of several B-specific proteins suggests that they are involved in negatively regulating Brr2, positioning the U6/5'ss helix, and stabilizing the B complex structure. Our results indicate significant differences between the early activation phase of human and yeast spliceosomes.

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Language(s): eng - English
 Dates: 2017-08-032017-08-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.cell.2017.07.011
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Title: Cell
Source Genre: Journal
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Pages: 24 Volume / Issue: 170 (4) Sequence Number: - Start / End Page: 701 - 713, e1 - e4 Identifier: -