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

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.

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 Creators:
Townsend, C.1, Author              
Leelaram, M. N.2, Author              
Agafonov, D. E.3, Author              
Dybkov, O.3, Author              
Will, C. L.3, Author              
Bertram, K.1, Author              
Urlaub, H.4, Author              
Kastner, B.3, Author              
Stark, Holger1, Author              
Lührmann, R.3, 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              
3Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
4Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2020-12-182020-12-18
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.abc3753
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Title: Science
Source Genre: Journal
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Pages: 13 Volume / Issue: 370 (6523) Sequence Number: eabc3753 Start / End Page: - Identifier: -