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Related Concept Videos

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Using the E1A Minigene Tool to Study mRNA Splicing Changes
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Split-APEX implicates splicing factor SRSF1 and splicing helicases in ribosomal biogenesis.

Vasileios Paschalis1,2, Max F K Wills1,2, Philippe De Gusmao Araujo1,2

  • 1Institute for Structural and Chemical Biology, University of Leicester, Leicester, United Kingdom.

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|January 5, 2026
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Summary

SR proteins, like SRSF1, are crucial for RNA splicing. New research reveals these proteins may also collaborate with RNA helicases in ribosomal assembly and translation, expanding their known cellular roles.

Keywords:
RNA splicing helicasesSRSF1ribosomal biogenesisspliceosomal assemblysplit-APEX

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • SR proteins are RNA-binding proteins essential for various cellular processes, including transcription and translation.
  • SRSF1, a well-known SR protein, is involved in RNA splicing and spliceosome assembly, interacting with RNA helicases like DDX23.

Purpose of the Study:

  • To investigate the role of SRSF1 in other steps of spliceosome assembly and reaction.
  • To identify proteins in proximity to SRSF1 during spliceosome dynamics using split-APEX technology.

Main Methods:

  • Utilized split-APEX proximity labeling with SRSF1 and various RNA helicases involved in different spliceosome steps.
  • Analyzed biotinylated proteins to identify SRSF1 interactors and proximal proteins in spliceosome complexes.

Main Results:

  • All tested helicases complemented SRSF1, indicating interactions or proximity.
  • Identified proximal proteins primarily belonged to two categories: splicing-related proteins and ribosomal proteins.
  • The proximity profiles were remarkably similar across different helicase interactions with SRSF1.

Conclusions:

  • SRSF1 and canonical helicases may have previously unrecognized collaborative functions in ribosomal assembly.
  • These findings suggest potential new roles for SR proteins and helicases in translation processes.
  • The study expands the understanding of SR protein involvement beyond splicing into ribosome biogenesis and translation.