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10.1038/ncomms10200 http://scihub22266oqcxt.onion/10.1038/ncomms10200 C4725763!4725763 !26725510     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26725510 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Commun 2016 ; 7 (ä): 10200 Nephropedia Template TP {{tp|p=26725510 |t=2016. Multistep assembly of DNA condensation clusters by SMC |pdf=|usr=}}{{26725510 }} gab.com Text Multistep assembly of DNA condensation clusters by SMC JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26725510 #FOAvip SMC (structural maintenance of chromosomes) family members play essential roles in chromosome condensation, sister chromatid cohesion and DNA repair. It remains unclear how SMCs structure chromosomes and how their mechanochemical cycle regulates their interactions with DNA. Here we used single-molecule fluorescence microscopy to visualize how Bacillus subtilis SMC (BsSMC) interacts with flow-stretched DNAs. We report that BsSMC can slide on DNA, switching between static binding and diffusion. At higher concentrations, BsSMCs form clusters that condense DNA in a weakly ATP-dependent manner. ATP increases the apparent cooperativity of DNA condensation, demonstrating that BsSMC can interact cooperatively through their ATPase head domains. Consistent with these results, ATPase mutants compact DNA more slowly than wild-type BsSMC in the presence of ATP. Our results suggest that transiently static BsSMC molecules can nucleate the formation of clusters that act to locally condense the chromosome while forming long-range DNA bridges. Twit Text FOAVip Multistep assembly of DNA condensation clusters by SMC ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26725510 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26725510 #FOAvip English Wikipedia <ref>{{Cite pmid|26725510 }}</ref> Multistep assembly of DNA condensation clusters by SMC #MMPMID26725510 Kim H ; Loparo JJ Nat Commun 2016[Jan]; 7 (ä): 10200 PMID26725510 show ga SMC (structural maintenance of chromosomes) family members play essential roles in chromosome condensation, sister chromatid cohesion and DNA repair. It remains unclear how SMCs structure chromosomes and how their mechanochemical cycle regulates their interactions with DNA. Here we used single-molecule fluorescence microscopy to visualize how Bacillus subtilis SMC (BsSMC) interacts with flow-stretched DNAs. We report that BsSMC can slide on DNA, switching between static binding and diffusion. At higher concentrations, BsSMCs form clusters that condense DNA in a weakly ATP-dependent manner. ATP increases the apparent cooperativity of DNA condensation, demonstrating that BsSMC can interact cooperatively through their ATPase head domains. Consistent with these results, ATPase mutants compact DNA more slowly than wild-type BsSMC in the presence of ATP. Our results suggest that transiently static BsSMC molecules can nucleate the formation of clusters that act to locally condense the chromosome while forming long-range DNA bridges. |Bacillus subtilis/genetics/*metabolism [MESH] |Bacterial Proteins/genetics/*metabolism [MESH] |Cell Cycle Proteins/genetics/*metabolism [MESH] |Chromosomes, Bacterial/*physiology [MESH] |DNA, Bacterial/*chemistry/genetics/metabolism [MESH] |Gene Expression Regulation, Bacterial/*physiology [MESH]Multistep assembly of DNA condensation clusters by SMC (epmc).pdf DeepDyve Pubget Overpricing