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10.1038/nchembio.2235 http://scihub22266oqcxt.onion/10.1038/nchembio.2235 C5161692!5161692!27870837     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Chem+Biol 2017 ; 13 (1): 105-10 Nephropedia Template TP {{tp|p=27870837|t=2017. Ubiquitin Utilizes an Acidic Surface Patch to Alter Chromatin Structure |pdf=|usr=}}{{27870837}} gab.com Text Ubiquitin Utilizes an Acidic Surface Patch to Alter Chromatin Structure JO: Nat Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=27870837 #FOAvip Ubiquitylation of histone H2B, associated with gene activation, leads to chromatin decompaction through an unknown mechanism. We used a hydrogen-deuterium exchange strategy coupled with nuclear magnetic resonance spectroscopy to map the ubiquitin surface responsible for its structural effects on chromatin. Our studies revealed that a previously uncharacterized acidic patch on ubiquitin comprising residues Glu16 and Glu18 is essential for decompaction. These residues mediate promiscuous electrostatic interactions with the basic histone proteins, potentially positioning the ubiquitin moiety as a dynamic ?wedge? that prevents the intimate association of neighboring nucleosomes. Using two independent cross-linking strategies and an oligomerization assay, we also showed that ubiquitin-ubiquitin contacts occur in the chromatin environment and are important for the solubilization of the chromatin polymers. Our work highlights a novel, chromatin-related aspect of the ?ubiquitin code?, and sheds light on how the information rich ubiquitin modification can orchestrate different biochemical outcomes using different surface features. Twit Text FOAVip Ubiquitin Utilizes an Acidic Surface Patch to Alter Chromatin Structure ????Nat Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=27870837 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27870837 #FOAvip English Wikipedia <ref>{{Cite pmid|27870837}}</ref> Ubiquitin Utilizes an Acidic Surface Patch to Alter Chromatin Structure #MMPMID27870837 Debelouchina GT; Gerecht K; Muir TW Nat Chem Biol 2017[Jan]; 13 (1): 105-10 PMID27870837show ga Ubiquitylation of histone H2B, associated with gene activation, leads to chromatin decompaction through an unknown mechanism. We used a hydrogen-deuterium exchange strategy coupled with nuclear magnetic resonance spectroscopy to map the ubiquitin surface responsible for its structural effects on chromatin. Our studies revealed that a previously uncharacterized acidic patch on ubiquitin comprising residues Glu16 and Glu18 is essential for decompaction. These residues mediate promiscuous electrostatic interactions with the basic histone proteins, potentially positioning the ubiquitin moiety as a dynamic ?wedge? that prevents the intimate association of neighboring nucleosomes. Using two independent cross-linking strategies and an oligomerization assay, we also showed that ubiquitin-ubiquitin contacts occur in the chromatin environment and are important for the solubilization of the chromatin polymers. Our work highlights a novel, chromatin-related aspect of the ?ubiquitin code?, and sheds light on how the information rich ubiquitin modification can orchestrate different biochemical outcomes using different surface features. äUbiquitin Utilizes an Acidic Surface Patch to Alter Chromatin Structur(epmc).pdf DeepDyve Pubget Overpricing