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Structural elucidation of a novel mechanism for the bacteriophage-based inhibition of the RNA degradosome

DOI: 10.7554/eLife.16413 DOI Help

Authors: An Van Den Bossche (Scientific Institute of Public Health, Brussels) , Steven Hardwick (University of Cambridge) , Pieter-Jan Ceyssens (Scientific Institute of Public Health, Brussels) , Hanne Hendrix (KU Leuven) , Marleen Voet (KU Leuven) , Tom Dendooven (KU Leuven) , Katarzyna J. Bandyra (University of Cambridge) , Marc De Maeyer (KU Leuven) , Abram Aertsen (KU Leuven) , Jean-Paul Noben (Transnational University Limburg) , Ben Luisi (Department of Biochemistry, University of Cambridge) , Rob Lavigne (KU Leuven)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Elife , VOL 5

State: Published (Approved)
Published: July 2016
Diamond Proposal Number(s): 9537

Open Access Open Access

Abstract: In all domains of life, the catalysed degradation of RNA facilitates rapid adaptation to changing environmental conditions, while destruction of foreign RNA is an important mechanism to prevent host infection. We have identified a virus-encoded protein termed gp37/Dip, which directly binds and inhibits the RNA degradation machinery of its bacterial host. Encoded by giant phage фKZ, this protein associates with two RNA binding sites of the RNase E component of the Pseudomonas aeruginosa RNA degradosome, occluding them from substrates and resulting in effective inhibition of RNA degradation and processing. The 2.2 Å crystal structure reveals that this novel homo-dimeric protein has no identifiable structural homologues. Our biochemical data indicate that acidic patches on the convex outer surface bind RNase E. Through the activity of Dip, фKZ has evolved a unique mechanism to down regulate a key metabolic process of its host to allow accumulation of viral RNA in infected cells.

Journal Keywords: Pseudomonas aeruginosa; RNA degradosome; RNA metabolism; bacteriophage; biochemistry; infectious disease; microbiology; protein-protein interactions; virus

Diamond Keywords: Bacteriophages; Viruses

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Added On: 23/08/2016 16:33

Documents:
elife-16413-v2.pdf

Discipline Tags:

Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)