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Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...
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Using the E1A Minigene Tool to Study mRNA Splicing Changes
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The tumour suppressor RBM5 activates the helicase DHX15 to regulate splicing.

Shiheng Liu1,2, Tiantian Su1, Jeffrey Huang1

  • 1Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, CA 90095, USA.

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The tumor suppressor RBM5 acts as a spliceosome gatekeeper, controlling apoptosis-regulating splicing. It physically blocks spliceosome progression while activating the DHX15 helicase to ensure tumor-suppressive alternative splicing.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cancer Biology

Background:

  • Pre-mRNA splicing is crucial for protein diversity and frequently altered in cancer.
  • The tumor suppressor RBM5 regulates apoptosis-related splicing but its mechanism is unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism of RBM5 in regulating pre-mRNA splicing.
  • To determine the structural basis of RBM5's interaction with the spliceosome.

Main Methods:

  • In vivo spliceosome capture combined with cryogenic electron microscopy (cryo-EM).
  • Functional assays to validate RBM5 interactions and their effect on splicing.

Main Results:

  • Structural determination of RBM5-bound spliceosomes at the U2 snRNP branchpoint recognition stage.
  • RBM5 was found to bind the SF3B1 HEAT surface, performing dual functions: steric blockage of spliceosome progression and activation of the DHX15 helicase.
  • RBM5's interaction with DHX15 is mediated by U2SURP/SR140, and disruption of RBM5 interfaces inhibits exon repression.

Conclusions:

  • RBM5 functions as a dual-action spliceosome gatekeeper, coupling helicase activation with physical stalling.
  • This mechanism enforces tumor-suppressive alternative splicing programs.
  • Mutations in RBM5 regulatory interfaces are common in cancer and likely disrupt its tumor-suppressive functions.