Structure of a transcribing Pol II-DSIF-SPT6-U1 snRNP complex

Luojia Zhang, Christopher Batters, Shintaro Aibara, Yuliya Gordiyenko, Kristina Žumer, Jana Schmitzová, Kerstin Maier, Patrick Cramer and Suyang Zhang ()
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Luojia Zhang: MRC Laboratory of Molecular Biology
Christopher Batters: MRC Laboratory of Molecular Biology
Shintaro Aibara: Max Planck Institute for Multidisciplinary Sciences, Department of Molecular Biology
Yuliya Gordiyenko: MRC Laboratory of Molecular Biology
Kristina Žumer: Max Planck Institute for Multidisciplinary Sciences, Department of Molecular Biology
Jana Schmitzová: Max Planck Institute for Multidisciplinary Sciences, Department of Molecular Biology
Kerstin Maier: Max Planck Institute for Multidisciplinary Sciences, Department of Molecular Biology
Patrick Cramer: Max Planck Institute for Multidisciplinary Sciences, Department of Molecular Biology
Suyang Zhang: MRC Laboratory of Molecular Biology

Nature Communications, 2025, vol. 16, issue 1, 1-10

Abstract: Abstract In eukaryotic cells, splicing occurs predominantly co-transcriptionally, enhancing splicing efficiency and fidelity while introducing an additional layer of regulation over gene expression. RNA polymerase II (Pol II) facilitates co-transcriptional splicing by recruiting the U1 small nuclear ribonucleoprotein particle (U1 snRNP) to the nascent transcripts. Here, we report the cryo-electron microscopy structure of a transcribing Pol II-U1 snRNP complex with elongation factors DSIF and SPT6. In addition, our biochemical analysis reveals that the phosphorylated Pol II carboxyl-terminal domain and SPT6 interact directly with U1 snRNP proteins, facilitating its recruitment to the elongation complex. This multivalent interaction between U1 snRNP and the transcription elongation complex may both allow efficient spliceosome assembly and ensure transcription processivity.

Date: 2025
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DOI: 10.1038/s41467-025-60979-9

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