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Journal Article

Molecular architecture of the human U4/U6.U5 tri-snRNP.

MPS-Authors
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Agafonov,  D. E.
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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Dybkov,  O.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Hofele,  R. V.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Liu,  W.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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

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Stark,  H.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

http://science.sciencemag.org/content/351/6280/1416
(Publisher version)

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Supplementary Material (public)

2253195_Suppl.htm
(Supplementary material), 51KB

2253195_Suppl_1.pdf
(Supplementary material), 6MB

2253195_Suppl_2.xlsx
(Supplementary material), 69KB

2253195_Suppl_3.mp4
(Supplementary material), 30MB

Citation

Agafonov, D. E., Kastner, B., Dybkov, O., Hofele, R. V., Liu, W., Urlaub, H., et al. (2016). Molecular architecture of the human U4/U6.U5 tri-snRNP. Science, 351(6280), 1416-1420. doi:10.1126/science.aad2085.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0029-C7F5-4
Abstract
The U4/U6.U5 triple small nuclear ribonucleoprotein (tri-snRNP) is a major spliceosome building block. Here we describe a 7 Å 3D structure of the 1.8 MDa human tri-snRNP obtained by single-particle electron cryomicroscopy. We fit all known high-resolution structures of tri-snRNP components into the EM density map and validated them by protein crosslinking. Our model reveals how the spatial organization of Brr2 RNA helicase prevents pre-mature U4/U6 RNA unwinding in isolated human tri-snRNPs and how the Sad1 protein likely tethers Brr2 to its pre-activation position. Comparison of our model with cryo-EM 3D structures of the S. cerevisiae tri-snRNP and S. pombe spliceosome indicates that Brr2 undergoes a dramatic conformational change during spliceosome activation, and that Prp8 is also rearranged to accommodate the spliceosome's catalytic RNA network.