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10.1021/acs.jpcb.5b09734 http://scihub22266oqcxt.onion/10.1021/acs.jpcb.5b09734 C5436045!5436045!26575591     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+B 2015 ; 119 (48): 15001-5 Nephropedia Template TP {{tp|p=26575591|t=2015. Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome |pdf=|usr=}}{{26575591}} gab.com Text Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome JO: J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=26575591 #FOAvip The nucleosome, comprising a histone protein core wrapped around by DNA, is the fundamental packing unit of DNA in cells. Lysine acetylation at the histone core elevates DNA accessibility in the nucleosome, the mechanism of which remains largely unknown. By employing our recently developed hybrid single molecule approach, here we report how the structural dynamics of DNA in the nucleosome is altered upon acetylation at histone H3 lysine 56 (H3K56) that is critical for elevated DNA accessibility. Our results indicate that H3K56 acetylation facilitates the structural dynamics of the DNA at the nucleosome termini that spontaneously and repeatedly open and close on a ms time scale. The results support a molecular mechanism of histone acetylation in catalyzing DNA unpacking whose efficiency is ultimately limited by the spontaneous DNA dynamics at the nucleosome temini. This study provides the first and unique experimental evidence revealing a role of protein chemical modification in directly regulating the kinetic stability of the DNA packing unit. Twit Text FOAVip Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome ????J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=26575591 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26575591 #FOAvip English Wikipedia <ref>{{Cite pmid|26575591}}</ref> Lysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleosome #MMPMID26575591 Kim J; Lee J; Lee TH J Phys Chem B 2015[Dec]; 119 (48): 15001-5 PMID26575591show ga The nucleosome, comprising a histone protein core wrapped around by DNA, is the fundamental packing unit of DNA in cells. Lysine acetylation at the histone core elevates DNA accessibility in the nucleosome, the mechanism of which remains largely unknown. By employing our recently developed hybrid single molecule approach, here we report how the structural dynamics of DNA in the nucleosome is altered upon acetylation at histone H3 lysine 56 (H3K56) that is critical for elevated DNA accessibility. Our results indicate that H3K56 acetylation facilitates the structural dynamics of the DNA at the nucleosome termini that spontaneously and repeatedly open and close on a ms time scale. The results support a molecular mechanism of histone acetylation in catalyzing DNA unpacking whose efficiency is ultimately limited by the spontaneous DNA dynamics at the nucleosome temini. This study provides the first and unique experimental evidence revealing a role of protein chemical modification in directly regulating the kinetic stability of the DNA packing unit. äLysine Acetylation Facilitates Spontaneous DNA Dynamics in the Nucleos(epmc).pdf DeepDyve Pubget Overpricing