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|Title: ||Structural elucidation of a novel mechanism for the bacteriophage-based inhibition of the RNA degradosome|
|Authors: ||Van den Bossche, An|
Hardwick, Steven W.
Bandyra, Katarzyna J.
De Maeyer, Marc
Luisi, Ben F.
|Issue Date: ||2016|
|Citation: ||ELIFE, 2016(5) (Art N° e16413)|
|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 A˚ 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.|
|Notes: ||[Van den Bossche, A.; Hendrix, H.; Voet, M.; Dendooven, T.; Lavigne, R.] Katholieke Univ Leuven, Lab Gene Technol, B-3001 Leuven, Belgium. [Hardwick, S. W.; Bandyra, K. J.; Luisi, B. F.] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England. [Van den Bossche, A.; Ceyssens, P-J] Sci Inst Publ Hlth WIV ISP, Div Bacterial Dis, B-1050 Brussels, Belgium. [De Maeyer, M.] Katholieke Univ Leuven, Biochem Mol & Struct Biol Sect, B-3001 Leuven, Belgium. [Aertsen, A.] Katholieke Univ Leuven, Food Microbiol Lab, B-3001 Leuven, Belgium. [Noben, J-P] Hasselt Univ, Biomed Res Inst, B-3950 Diepenbeek, Belgium. [Noben, J-P] Hasselt Univ, Transnat Univ Limburg, B-3950 Diepenbeek, Belgium.|
|ISI #: ||000380845900001|
|Type: ||Journal Contribution|
|Validation: ||ecoom, 2017|
|Appears in Collections: ||Research publications|
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