Journal
SCIENCE
Volume 371, Issue 6526, Pages 305-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abf1870
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Funding
- EMBO [ALTF 830-2018]
- H2020 Marie Curie Individual Fellowship [894862]
- Deutsche Forschungsgemeinschaft [EXC 2067/1390729940]
- European Research Council Advanced Investigator Grant CHROMATRANS [882357]
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The study revealed that RNA polymerase II interacts directly with U1 small nuclear ribonucleoprotein particle, facilitating the positioning of the pre-mRNA splice site and the formation of an intron loop to aid in spliceosome assembly.
To initiate cotranscriptional splicing, RNA polymerase II (Pol II) recruits the U1 small nuclear ribonucleoprotein particle (U1 snRNP) to nascent precursor messenger RNA (pre-mRNA). Here, we report the cryo-electron microscopy structure of a mammalian transcribing Pol II-U1 snRNP complex. The structure reveals that Pol II and U1 snRNP interact directly. This interaction positions the pre-mRNA 5' splice site near the RNA exit site of Pol II. Extension of pre-mRNA retains the 5' splice site, leading to the formation of a growing intron loop. Loop formation may facilitate scanning of nascent pre-mRNA for the 3' splice site, functional pairing of distant intron ends, and prespliceosome assembly. Our results provide a starting point for a mechanistic analysis of cotranscriptional spliceosome assembly and the biogenesis of mRNA isoforms by alternative splicing.
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