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Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation

MPG-Autoren
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Townsend,  C.
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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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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Will,  C. L.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Bertram,  K.
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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Kastner,  B.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Stark,  Holger
Department of Structural Dynamics, 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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Zitation

Townsend, C., Leelaram, M. N., Agafonov, D. E., Dybkov, O., Will, C. L., Bertram, K., et al. (2020). Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. Science, 370(6523): eabc3753. doi:10.1126/science.abc3753.


Zitierlink: https://hdl.handle.net/21.11116/0000-0008-6F90-9
Zusammenfassung
Spliceosome activation involves extensive protein and RNA rearrangements that lead to formation of a catalytically active U2/U6 RNA structure. At present, little is known about the assembly pathway of the latter and the mechanism whereby proteins aid its proper folding. Here, we report the cryo–electron microscopy structures of two human, activated spliceosome precursors (that is, pre-Bact complexes) at core resolutions of 3.9 and 4.2 angstroms. These structures elucidate the order of the numerous protein exchanges that occur during activation, the mutually exclusive interactions that ensure the correct order of ribonucleoprotein rearrangements needed to form the U2/U6 catalytic RNA, and the stepwise folding pathway of the latter. Structural comparisons with mature Bact complexes reveal the molecular mechanism whereby a conformational change in the scaffold protein PRP8 facilitates final three-dimensional folding of the U2/U6 catalytic RNA.