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  Structure and conformational dynamics of the human spliceosomal Bact complex.

Haselbach, D., Komarov, I., Agafonov, D. E., Hartmuth, K., Graf, B., Dybkov, O., et al. (2018). Structure and conformational dynamics of the human spliceosomal Bact complex. Cell, 172(3), 454-464, e1-e5. doi:10.1016/j.cell.2018.01.010.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-3A6F-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-6499-0
Genre: Journal Article

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 Creators:
Haselbach, D.1, Author              
Komarov, I.2, Author              
Agafonov, D. E.2, Author              
Hartmuth, K.2, Author              
Graf, B.1, Author              
Dybkov, O.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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 Abstract: The spliceosome is a highly dynamic macromolecular complex that precisely excises introns from pre-mRNA. Here we report the cryo-EM 3D structure of the human Bact spliceosome at 3.4 Å resolution. In the Bact state, the spliceosome is activated but not catalytically primed, so that it is functionally blocked prior to the first catalytic step of splicing. The spliceosomal core is similar to the yeast Bact spliceosome; important differences include the presence of the RNA helicase aquarius and peptidyl prolyl isomerases. To examine the overall dynamic behavior of the purified spliceosome, we developed a principal component analysis-based approach. Calculating the energy landscape revealed eight major conformational states, which we refined to higher resolution. Conformational differences of the highly flexible structural components between these eight states reveal how spliceosomal components contribute to the assembly of the spliceosome, allowing it to generate a dynamic interaction network required for its subsequent catalytic activation.

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Language(s): eng - English
 Dates: 2018-01-172018-01-25
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.cell.2018.01.010
 Degree: -

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Title: Cell
Source Genre: Journal
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Pages: - Volume / Issue: 172 (3) Sequence Number: - Start / End Page: 454 - 464, e1-e5 Identifier: -