+検索条件
-Structure paper
タイトル | Structural basis of branch site recognition by the human spliceosome. |
---|---|
ジャーナル・号・ページ | Science, Vol. 375, Issue 6576, Page 50-57, Year 2022 |
掲載日 | 2022年1月7日 |
著者 | Jonas Tholen / Michal Razew / Felix Weis / Wojciech P Galej / |
PubMed 要旨 | 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 ...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 17 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. |
リンク | Science / PubMed:34822310 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.05 - 3.3 Å |
構造データ | EMDB-13793: Human 17S U2 snRNP 5' domain core EMDB-13810: EMDB-13811, PDB-7q4o: EMDB-13812, PDB-7q4p: EMDB-13813: EMDB-13814: EMDB-13815: |
化合物 | ChemComp-ZN: ChemComp-HOH: |
由来 |
|
キーワード | NUCLEAR PROTEIN / snRNP / Spliceosome / U2 snRNP / Splicing |