<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">An Van den Bossche</style></author><author><style face="normal" font="default" size="100%">Hardwick, Steven W</style></author><author><style face="normal" font="default" size="100%">Pieter-Jan Ceyssens</style></author><author><style face="normal" font="default" size="100%">Hendrix, Hanne</style></author><author><style face="normal" font="default" size="100%">Voet, Marleen</style></author><author><style face="normal" font="default" size="100%">Dendooven, Tom</style></author><author><style face="normal" font="default" size="100%">Bandyra, Katarzyna J</style></author><author><style face="normal" font="default" size="100%">De Maeyer, Marc</style></author><author><style face="normal" font="default" size="100%">Aertsen, Abram</style></author><author><style face="normal" font="default" size="100%">Noben, Jean-Paul</style></author><author><style face="normal" font="default" size="100%">Luisi, Ben F</style></author><author><style face="normal" font="default" size="100%">Lavigne, Rob</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural elucidation of a novel mechanism for the bacteriophage-based inhibition of the RNA degradosome.</style></title><secondary-title><style face="normal" font="default" size="100%">Elife</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Elife</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Binding Sites</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystallography, X-Ray</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoribonucleases</style></keyword><keyword><style  face="normal" font="default" size="100%">Host-Parasite Interactions</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Multienzyme Complexes</style></keyword><keyword><style  face="normal" font="default" size="100%">Polyribonucleotide Nucleotidyltransferase</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Multimerization</style></keyword><keyword><style  face="normal" font="default" size="100%">Pseudomonas aeruginosa</style></keyword><keyword><style  face="normal" font="default" size="100%">Pseudomonas Phages</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA Helicases</style></keyword><keyword><style  face="normal" font="default" size="100%">Viral Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2016 Jul 22</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">5</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;
</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/27447594?dopt=Abstract</style></custom1></record></records></xml>