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-Structure paper
Title | Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. |
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Journal, issue, pages | Science, Vol. 370, Issue 6523, Year 2020 |
Publish date | Dec 18, 2020 |
Authors | Cole Townsend / Majety N Leelaram / Dmitry E Agafonov / Olexandr Dybkov / Cindy L Will / Karl Bertram / Henning Urlaub / Berthold Kastner / Holger Stark / Reinhard Lührmann / |
PubMed 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 ...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-B 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 B 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. |
External links | Science / PubMed:33243851 |
Methods | EM (single particle) |
Resolution | 3.9 - 8.0 Å |
Structure data | EMDB-11693, PDB-7aav: EMDB-11694, PDB-7abf: EMDB-11695, PDB-7abg: EMDB-11696, PDB-7abh: EMDB-11697, PDB-7abi: |
Chemicals | ChemComp-GTP: ChemComp-MG: ChemComp-KGN: ChemComp-IHP: ChemComp-GTG: |
Source |
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Keywords | SPLICING / Complex / spliceosome / catalytic activation |