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10.1371/journal.pone.0177097 http://scihub22266oqcxt.onion/10.1371/journal.pone.0177097 C5435312!5435312!28520746     free     free     free       PLoS+One 2017 ; 12 (5): ä Nephropedia Template TP {{tp|p=28520746|t=2017. DNA recognition by an RNA-guided bacterial Argonaute |pdf=|usr=}}{{28520746}} gab.com Text DNA recognition by an RNA-guided bacterial Argonaute JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=28520746 #FOAvip Argonaute (Ago) proteins are widespread in prokaryotes and eukaryotes and share a four-domain architecture capable of RNA- or DNA-guided nucleic acid recognition. Previous studies identified a prokaryotic Argonaute protein from the eubacterium Marinitoga piezophila (MpAgo), which binds preferentially to 5?-hydroxylated guide RNAs and cleaves single-stranded RNA (ssRNA) and DNA (ssDNA) targets. Here we present a 3.2 Å resolution crystal structure of MpAgo bound to a 21-nucleotide RNA guide and a complementary 21-nucleotide ssDNA substrate. Comparison of this ternary complex to other target-bound Argonaute structures reveals a unique orientation of the N-terminal domain, resulting in a straight helical axis of the entire RNA-DNA heteroduplex through the central cleft of the protein. Additionally, mismatches introduced into the heteroduplex reduce MpAgo cleavage efficiency with a symmetric profile centered around the middle of the helix. This pattern differs from the canonical mismatch tolerance of other Argonautes, which display decreased cleavage efficiency for substrates bearing sequence mismatches to the 5? region of the guide strand. This structural analysis of MpAgo bound to a hybrid helix advances our understanding of the diversity of target recognition mechanisms by Argonaute proteins. Twit Text FOAVip DNA recognition by an RNA-guided bacterial Argonaute ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=28520746 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28520746 #FOAvip English Wikipedia <ref>{{Cite pmid|28520746}}</ref> DNA recognition by an RNA-guided bacterial Argonaute #MMPMID28520746 Doxzen KW; Doudna JA PLoS One 2017[]; 12 (5): ä PMID28520746show ga Argonaute (Ago) proteins are widespread in prokaryotes and eukaryotes and share a four-domain architecture capable of RNA- or DNA-guided nucleic acid recognition. Previous studies identified a prokaryotic Argonaute protein from the eubacterium Marinitoga piezophila (MpAgo), which binds preferentially to 5?-hydroxylated guide RNAs and cleaves single-stranded RNA (ssRNA) and DNA (ssDNA) targets. Here we present a 3.2 Å resolution crystal structure of MpAgo bound to a 21-nucleotide RNA guide and a complementary 21-nucleotide ssDNA substrate. Comparison of this ternary complex to other target-bound Argonaute structures reveals a unique orientation of the N-terminal domain, resulting in a straight helical axis of the entire RNA-DNA heteroduplex through the central cleft of the protein. Additionally, mismatches introduced into the heteroduplex reduce MpAgo cleavage efficiency with a symmetric profile centered around the middle of the helix. This pattern differs from the canonical mismatch tolerance of other Argonautes, which display decreased cleavage efficiency for substrates bearing sequence mismatches to the 5? region of the guide strand. This structural analysis of MpAgo bound to a hybrid helix advances our understanding of the diversity of target recognition mechanisms by Argonaute proteins. äDNA recognition by an RNA-guided bacterial Argonaute (epmc).pdf DeepDyve Pubget Overpricing