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Viral interference of bacterial RNA metabolism machinery

Journal Contribution - Journal Article

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 two 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.
Journal: RNA Biology
ISSN: 1547-6286
Issue: 1
Volume: 14
Pages: 6 - 10
Publication year:2017
Keywords:bacteriophage, phage-host interaction, pseudomonas aeruginosa, RNA degradosome, RNase E