9QEQ

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

This is a non-PDB format compatible entry.

Summary for 9QEQ

• Entry DOI: 10.2210/pdb9qeq/pdb
• EMDB information: 53087
• Descriptor: DNA-directed RNA polymerase subunit, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, ... (30 entities in total)
• Functional Keywords: transcription, splicing, elongation, cryo-em
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 28
• Total formula weight: 1132737.39

Authors

Zhang, S. (deposition date: 2025-03-10, release date: 2025-07-09, Last modification date: 2025-07-16)

Primary citation

Zhang, L.,Batters, C.,Aibara, S.,Gordiyenko, Y.,Zumer, K.,Schmitzova, J.,Maier, K.,Cramer, P.,Zhang, S.
Structure of a transcribing Pol II-DSIF-SPT6-U1 snRNP complex.
Nat Commun, 16:5823-5823, 2025

PubMed 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.

PubMed: 40595577
DOI: 10.1038/s41467-025-60979-9

Experimental method

ELECTRON MICROSCOPY (3.5 Å)