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Structural basis of branch site recognition by the human spliceosome

Recognition of the intron branch site (BS) by the U2 small nuclear ribonucleoprotein (snRNP) is a critical event during spliceosome assembly. In mammals, BS sequences are poorly conserved, and unambiguous intron recognition cannot be achieved solely through a base-pairing mechanism. We isolated huma...

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Hauptverfasser: Tholen, Jonas (VerfasserIn) , Razew, Michal (VerfasserIn) , Weis, Felix (VerfasserIn) , Galej, Wojciech P. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2022
In: Science
Year: 2022, Jahrgang: 375, Heft: 6576, Pages: 50-57
ISSN:1095-9203
DOI:10.1126/science.abm4245
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1126/science.abm4245
Verlag, lizenzpflichtig, Volltext: https://www.science.org/doi/10.1126/science.abm4245
Volltext
Verfasserangaben:Jonas Tholen, Michal Razew, Felix Weis, Wojciech P. Galej

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520 |a Recognition of the intron branch site (BS) by the U2 small nuclear ribonucleoprotein (snRNP) is a critical event during spliceosome assembly. In mammals, BS sequences are poorly conserved, and unambiguous intron recognition cannot be achieved solely through a base-pairing mechanism. We isolated human 17S U2 snRNP and reconstituted in vitro its adenosine 5´-triphosphate (ATP)–dependent remodeling and binding to the pre–messenger RNA substrate. We determined a series of high-resolution (2.0 to 2.2 angstrom) structures providing snapshots of the BS selection process. The substrate-bound U2 snRNP shows that SF3B6 stabilizes the BS:U2 snRNA duplex, which could aid binding of introns with poor sequence complementarity. ATP-dependent remodeling uncoupled from substrate binding captures U2 snRNA in a conformation that competes with BS recognition, providing a selection mechanism based on branch helix stability. 
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