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

MPG-Autoren
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Bertram,  K.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Agafonov,  D. E.
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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Haselbach,  D.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Leelaram,  M. N.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Will,  C. L.
Department of Cellular Biochemistry, 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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Kastner,  B.
Department of Cellular Biochemistry, 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;

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Zitation

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): e11. doi:10.1016/j.cell.2017.07.011.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002D-B9FC-3
Zusammenfassung
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.