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Human ribosomal protein S26 suppresses the splicing of its pre-mRNA

Anton V Ivanov1, Alexey A Malygin, Galina G Karpova

  • 1Laboratory of Structure and Function of Ribosomes, Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, pr. Lavrentieva, 8, Novosibirsk, 630090, Russia.

Biochimica Et Biophysica Acta
|February 18, 2005
PubMed

Insights

Ribosomal protein S26 (rpS26) binds to its own pre-mRNA and suppresses both conventional and alternative splicing. This interaction was mapped to specific sites on the rpS26 pre-mRNA secondary structure.

Area of Science:

  • Molecular Biology
  • RNA Splicing
  • Gene Regulation

Background:

  • Ribosomal proteins play crucial roles beyond translation, including roles in RNA processing.
  • Ribosomal protein S26 (rpS26) has been implicated in various cellular functions.
  • Understanding the specific interactions of rpS26 with its own pre-mRNA is essential for elucidating its regulatory roles.

Purpose of the Study:

  • To investigate the interaction between human ribosomal protein S26 (rpS26) and its pre-mRNA.
  • To determine the effect of rpS26 on the splicing of its own pre-mRNA.
  • To map the binding sites of rpS26 on the pre-mRNA molecule.

Main Methods:

  • In vitro binding assays using recombinant and endogenous rpS26 with rpS26 pre-mRNA fragments.
  • In vitro splicing assays of rpS26 pre-mRNA.
  • Toe-printing analysis to map rpS26 binding sites on pre-mRNA secondary structure.

Main Results:

  • Human recombinant rpS26 interacts with rpS26 pre-mRNA intron I and mRNA fragments.
  • Endogenous rpS26 in HeLa nuclear extract also binds to intron I and mRNA fragments.
  • Recombinant rpS26 addition enhanced binding and suppressed the formation of both conventional and alternative spliced mRNAs.
  • Toe-printing identified two clusters of nucleotides on the pre-mRNA secondary structure involved in rpS26 binding, associated with conventional and alternative 3' splice sites.

Conclusions:

  • rpS26 directly interacts with its pre-mRNA, influencing its own splicing.
  • rpS26 acts as a suppressor of both conventional and alternative splicing pathways for its pre-mRNA.
  • The binding of rpS26 to specific sites on its pre-mRNA is critical for regulating its splicing outcomes.

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