Journal
SCIENCE
Volume 375, Issue 6576, Pages 50-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abm4245
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Funding
- European Research Council (ERC) under the European Union [950278]
- EMBL Interdisciplinary Postdoc (EIPOD) programme under Marie Sklodowska-Curie Actions COFUND [847543]
- European Research Council (ERC) [950278] Funding Source: European Research Council (ERC)
- Marie Curie Actions (MSCA) [847543] Funding Source: Marie Curie Actions (MSCA)
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Recognition of intron branch site by U2 snRNP is a critical event during spliceosome assembly. The stability of BS:U2 snRNA duplex, aided by SF3B6, is important for binding introns with poor sequence complementarity. ATP-dependent remodeling captures U2 snRNA in a conformation that competes with BS recognition, providing a mechanism based on branch helix stability.
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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