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10.1101/cshperspect.a023192 http://scihub22266oqcxt.onion/10.1101/cshperspect.a023192 C4142969!4142969!25183833     free     free     free       Cold+Spring+Harb+Perspect+Biol 2014 ; 6 (9): ä Nephropedia Template TP {{tp|p=25183833|t=2014. Holliday Junction Resolvases |pdf=|usr=}}{{25183833}} gab.com Text Holliday Junction Resolvases JO: Cold Spring Harb Perspect Biol http://www.kidney.de/pget.php?&tw=1&pmid=25183833 #FOAvip Four-way DNA intermediates, called Holliday junctions (HJs), can form during meiotic and mitotic recombination, and their removal is crucial for chromosome segregation. A group of ubiquitous and highly specialized structure-selective endonucleases catalyze the cleavage of HJs into two disconnected DNA duplexes in a reaction called HJ resolution. These enzymes, called HJ resolvases, have been identified in bacteria and their bacteriophages, archaea, and eukaryotes. In this review, we discuss fundamental aspects of the HJ structure and their interaction with junction-resolving enzymes. This is followed by a brief discussion of the eubacterial RuvABC enzymes, which provide the paradigm for HJ resolvases in other organisms. Finally, we review the biochemical and structural properties of some well-characterized resolvases from archaea, bacteriophage, and eukaryotes. Twit Text FOAVip Holliday Junction Resolvases ????Cold Spring Harb Perspect Biol http://www.kidney.de/pget.php?&tw=1&pmid=25183833 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25183833 #FOAvip English Wikipedia <ref>{{Cite pmid|25183833}}</ref> Holliday Junction Resolvases #MMPMID25183833 Wyatt HD; West SC Cold Spring Harb Perspect Biol 2014[Sep]; 6 (9): ä PMID25183833show ga Four-way DNA intermediates, called Holliday junctions (HJs), can form during meiotic and mitotic recombination, and their removal is crucial for chromosome segregation. A group of ubiquitous and highly specialized structure-selective endonucleases catalyze the cleavage of HJs into two disconnected DNA duplexes in a reaction called HJ resolution. These enzymes, called HJ resolvases, have been identified in bacteria and their bacteriophages, archaea, and eukaryotes. In this review, we discuss fundamental aspects of the HJ structure and their interaction with junction-resolving enzymes. This is followed by a brief discussion of the eubacterial RuvABC enzymes, which provide the paradigm for HJ resolvases in other organisms. Finally, we review the biochemical and structural properties of some well-characterized resolvases from archaea, bacteriophage, and eukaryotes. äHolliday Junction Resolvases (epmc).pdf DeepDyve Pubget Overpricing