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Interaction of Bacillus subtilis Polynucleotide Phosphorylase and RNase Y: STRUCTURAL MAPPING AND EFFECT ON mRNA

Elizabeth Salvo1, Shanique Alabi1, Bo Liu1

  • 1From the Department of Pharmacology and Systems Therapeutics, Icahn School of Medicine at Mount Sinai, New York, New York 10029.

The Journal of Biological Chemistry
|January 23, 2016
PubMed

Insights

Polynucleotide phosphorylase (PNPase) and RNase Y interaction in Bacillus subtilis mRNA decay was investigated. Disrupting this interaction did not significantly affect the turnover of two specific mRNAs examined.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Polynucleotide phosphorylase (PNPase) is the primary enzyme for Bacillus subtilis mRNA turnover.
  • Recent studies suggest a degradosome-like complex involving RNase Y and PNPase.
  • The specific role of the PNPase-RNase Y interaction in PNPase's exonucleolytic function requires clarification.

Purpose of the Study:

  • To investigate the role of the PNPase-RNase Y interaction in Bacillus subtilis mRNA decay.
  • To construct a bacterial strain with catalytically active PNPase incapable of interacting with RNase Y.

Main Methods:

  • Homology modeling of Bacillus subtilis PNPase based on E. coli PNPase structure.
  • Site-directed mutagenesis to disrupt PNPase-RNase Y interaction.
  • Analysis of mRNA decay profiles in engineered bacterial strains.

Main Results:

  • Mutations predicted to disrupt RNase Y binding resulted in a loss of interaction.
  • Disrupting the PNPase-RNase Y interaction did not affect the turnover of two tested mRNAs.
  • Catalytically inactive PNPase still interacted with RNase Y.

Conclusions:

  • The interaction between PNPase and RNase Y may not be essential for the decay of all target mRNAs.
  • Further research is needed to fully elucidate the functional significance of the PNPase-RNase Y complex in mRNA turnover.
Keywords:
Bacillus subtilisPNPaseRNA turnoverRNase Ybacterial geneticsendonucleasemRNA decayphosphorylase

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