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10.1074/jbc.M114.591644 http://scihub22266oqcxt.onion/10.1074/jbc.M114.591644 C4256319!4256319 !25294883     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25294883 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2014 ; 289 (49 ): 33827-37 Nephropedia Template TP {{tp|p=25294883 |t=2014. Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions |pdf=|usr=}}{{25294883 }} gab.com Text Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25294883 #FOAvip The structure of eukaryotic chromatin directly influences gene function, and is regulated by chemical modifications of the core histone proteins. Modification of the human histone H4 N-terminal tail region by the small ubiquitin-like modifier protein, SUMO-3, is associated with transcription repression. However, the direct effect of sumoylation on chromatin structure and function remains unknown. Therefore, we employed a disulfide-directed strategy to generate H4 homogenously and site-specifically sumoylated at Lys-12 (suH4ss). Chromatin compaction and oligomerization assays with nucleosomal arrays containing suH4ss established that SUMO-3 inhibits array folding and higher order oligomerization, which underlie chromatin fiber formation. Moreover, the effect of sumoylation differed from that of acetylation, and could be recapitulated with the structurally similar protein ubiquitin. Mechanistic studies at the level of single nucleosomes revealed that, unlike acetylation, the effect of SUMO-3 arises from the attenuation of long-range internucleosomal interactions more than from the destabilization of a compacted dinucleosome state. Altogether, our results present the first insight on the direct structural effects of histone H4 sumoylation and reveal a novel mechanism by which SUMO-3 inhibits chromatin compaction. Twit Text FOAVip Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25294883 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25294883 #FOAvip English Wikipedia <ref>{{Cite pmid|25294883 }}</ref> Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions #MMPMID25294883 Dhall A ; Wei S ; Fierz B ; Woodcock CL ; Lee TH ; Chatterjee C J Biol Chem 2014[Dec]; 289 (49 ): 33827-37 PMID25294883 show ga The structure of eukaryotic chromatin directly influences gene function, and is regulated by chemical modifications of the core histone proteins. Modification of the human histone H4 N-terminal tail region by the small ubiquitin-like modifier protein, SUMO-3, is associated with transcription repression. However, the direct effect of sumoylation on chromatin structure and function remains unknown. Therefore, we employed a disulfide-directed strategy to generate H4 homogenously and site-specifically sumoylated at Lys-12 (suH4ss). Chromatin compaction and oligomerization assays with nucleosomal arrays containing suH4ss established that SUMO-3 inhibits array folding and higher order oligomerization, which underlie chromatin fiber formation. Moreover, the effect of sumoylation differed from that of acetylation, and could be recapitulated with the structurally similar protein ubiquitin. Mechanistic studies at the level of single nucleosomes revealed that, unlike acetylation, the effect of SUMO-3 arises from the attenuation of long-range internucleosomal interactions more than from the destabilization of a compacted dinucleosome state. Altogether, our results present the first insight on the direct structural effects of histone H4 sumoylation and reveal a novel mechanism by which SUMO-3 inhibits chromatin compaction. |*Protein Processing, Post-Translational [MESH] |Acetylation [MESH] |Chromatin Assembly and Disassembly [MESH] |Disulfides/chemistry [MESH] |Escherichia coli/genetics/metabolism [MESH] |Histones/*chemistry/genetics/metabolism [MESH] |Humans [MESH] |Kinetics [MESH] |Lysine/*chemistry/metabolism [MESH] |Models, Molecular [MESH] |Nucleosomes/*chemistry/genetics/metabolism [MESH] |Recombinant Proteins/chemistry/genetics/metabolism [MESH] |Signal Transduction [MESH] |Sumoylation [MESH] |Transcription, Genetic [MESH]Sumoylated human histone H4 prevents chromatin compaction by inhibitin(epmc).pdf DeepDyve Pubget Overpricing