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Functional link between DEAH/RHA helicase Prp43 activation and ATP base binding.

Julien Robert-Paganin1, Maral Halladjian2, Magali Blaud1

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The DEAH box helicase Prp43

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Prp43 is a bifunctional enzyme crucial for ribosome biogenesis and RNA splicing.
  • G-patch proteins activate Prp43's enzymatic activity through an unclear mechanism.

Purpose of the Study:

  • Investigate the mechanism of G-patch protein-mediated activation of Prp43.
  • Elucidate the role of nucleotide binding and specific motifs in Prp43 activity and regulation.

Main Methods:

  • Site-directed mutagenesis of Prp43 (R159A, F357A).
  • Biochemical assays to measure NTPase and helicase activities.
  • Phenotypic analysis of Prp43 mutants in the context of G-patch protein Gno1.

Main Results:

  • The unique nucleotide binding mode, with ATP base stacking between R159 (R-motif) and F357 (F-motif), is key for Prp43 function.
  • Mutating F357 decouples NTPase and helicase activities, while mutating R159 reduces both.
  • The R-motif mutant mimics the phenotype of Gno1 absence, indicating failed Prp43 activation.

Conclusions:

  • Nucleotide base stacking with R- and F-motifs is essential for Prp43 activity and regulation.
  • G-patch proteins likely activate Prp43 by facilitating this specific nucleotide binding interaction.
  • Understanding this mechanism provides insights into ribosome biogenesis and RNA splicing regulation.