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10.7554/eLife.22510 http://scihub22266oqcxt.onion/10.7554/eLife.22510 C5391205!5391205!28332978     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28332978&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2017 ; 6 (ä): ä Nephropedia Template TP {{tp|p=28332978|t=2017. Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes |pdf=|usr=}}{{28332978}} gab.com Text Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=28332978 #FOAvip The yeast Chd1 protein acts to position nucleosomes across genomes. Here, we model the structure of the Chd1 protein in solution and when bound to nucleosomes. In the apo state, the DNA-binding domain contacts the edge of the nucleosome while in the presence of the non-hydrolyzable ATP analog, ADP-beryllium fluoride, we observe additional interactions between the ATPase domain and the adjacent DNA gyre 1.5 helical turns from the dyad axis of symmetry. Binding in this conformation involves unravelling the outer turn of nucleosomal DNA and requires substantial reorientation of the DNA-binding domain with respect to the ATPase domains. The orientation of the DNA-binding domain is mediated by sequences in the N-terminus and mutations to this part of the protein have positive and negative effects on Chd1 activity. These observations indicate that the unfavorable alignment of C-terminal DNA-binding region in solution contributes to an auto-inhibited state.DOI:http://dx.doi.org/10.7554/eLife.22510.001 Twit Text FOAVip Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=28332978 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28332978 #FOAvip English Wikipedia <ref>{{Cite pmid|28332978}}</ref> Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes #MMPMID28332978 Sundaramoorthy R; Hughes AL; Singh V; Wiechens N; Ryan DP; El-Mkami H; Petoukhov M; Svergun DI; Treutlein B; Quack S; Fischer M; Michaelis J; Böttcher B; Norman DG; Owen-Hughes T eLife 2017[]; 6 (ä): ä PMID28332978show ga The yeast Chd1 protein acts to position nucleosomes across genomes. Here, we model the structure of the Chd1 protein in solution and when bound to nucleosomes. In the apo state, the DNA-binding domain contacts the edge of the nucleosome while in the presence of the non-hydrolyzable ATP analog, ADP-beryllium fluoride, we observe additional interactions between the ATPase domain and the adjacent DNA gyre 1.5 helical turns from the dyad axis of symmetry. Binding in this conformation involves unravelling the outer turn of nucleosomal DNA and requires substantial reorientation of the DNA-binding domain with respect to the ATPase domains. The orientation of the DNA-binding domain is mediated by sequences in the N-terminus and mutations to this part of the protein have positive and negative effects on Chd1 activity. These observations indicate that the unfavorable alignment of C-terminal DNA-binding region in solution contributes to an auto-inhibited state.DOI:http://dx.doi.org/10.7554/eLife.22510.001 äStructural reorganization of the chromatin remodeling enzyme Chd1 upon(epmc).pdf DeepDyve Pubget Overpricing