Viral interference of the bacterial RNA metabolism machinery

RNA Biol. 2017 Jan 2;14(1):6-10. doi: 10.1080/15476286.2016.1251003. Epub 2016 Nov 11.

Abstract

In a recent publication, we reported a unique interaction between a protein encoded by the giant myovirus phiKZ and the Pseudomonas aeruginosa RNA degradosome. Crystallography, site-directed mutagenesis and interactomics approaches revealed this 'degradosome interacting protein' or Dip, to adopt an 'open-claw' dimeric structure that presents acidic patches on its outer surface which hijack 2 conserved RNA binding sites on the scaffold domain of the RNase E component of the RNA degradosome. This interaction prevents substrate RNAs from being bound and degraded by the RNA degradosome during the virus infection cycle. In this commentary, we provide a perspective into the biological role of Dip, its structural analysis and its mysterious evolutionary origin, and we suggest some therapeutic and biotechnological applications of this distinctive viral protein.

Keywords: Bacteriophage; Pseudomonas aeruginosa; RNA degradosome; RNase E; phage-host interaction.

Publication types

  • Review

MeSH terms

  • Bacteria / drug effects
  • Bacteria / genetics*
  • Bacteria / metabolism
  • Bacteria / virology*
  • Bacteriophages / physiology*
  • Endoribonucleases / genetics
  • Endoribonucleases / metabolism
  • Host-Pathogen Interactions / genetics*
  • Multienzyme Complexes / genetics
  • Multienzyme Complexes / metabolism
  • Polyribonucleotide Nucleotidyltransferase / genetics
  • Polyribonucleotide Nucleotidyltransferase / metabolism
  • Protein Binding
  • Pseudomonas aeruginosa / physiology
  • Pseudomonas aeruginosa / virology
  • RNA Helicases / genetics
  • RNA Helicases / metabolism
  • RNA Stability
  • RNA, Bacterial / genetics*
  • RNA, Bacterial / metabolism

Substances

  • Multienzyme Complexes
  • RNA, Bacterial
  • degradosome
  • Polyribonucleotide Nucleotidyltransferase
  • Endoribonucleases
  • RNA Helicases