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

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Co-transcriptional splicing in eukaryotic cells is regulated by RNA polymerase II (Pol II) and U1 small nuclear ribonucleoprotein particle (U1 snRNP). We reveal the structure and interactions that facilitate this crucial gene expression process.

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Area of Science:

  • Molecular Biology
  • Gene Expression Regulation
  • Structural Biology

Background:

  • Splicing in eukaryotic cells predominantly occurs co-transcriptionally.
  • This process enhances splicing efficiency and fidelity.
  • RNA polymerase II (Pol II) recruits U1 small nuclear ribonucleoprotein particle (U1 snRNP) to nascent transcripts for co-transcriptional splicing.

Purpose of the Study:

  • To determine the structural basis of U1 snRNP recruitment to the transcription elongation complex.
  • To elucidate the role of elongation factors DSIF and SPT6 in this process.
  • To understand how these interactions regulate gene expression.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of the transcribing Pol II-U1 snRNP complex.
  • Biochemical analysis to investigate protein-protein interactions.

Main Results:

  • The cryo-EM structure of the transcribing Pol II-U1 snRNP complex with DSIF and SPT6 was determined.
  • Phosphorylated Pol II C-terminal domain and SPT6 directly interact with U1 snRNP proteins.
  • This interaction facilitates U1 snRNP recruitment to the elongation complex.

Conclusions:

  • Multivalent interactions between U1 snRNP and the transcription elongation complex are crucial for co-transcriptional splicing.
  • These interactions likely ensure efficient spliceosome assembly and transcription processivity.
  • This provides mechanistic insight into the regulation of gene expression.