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10.1093/nar/gkv620 http://scihub22266oqcxt.onion/10.1093/nar/gkv620 C4513879!4513879!26101253     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nucleic+Acids+Res 2015 ; 43 (13): 6596-606 Nephropedia Template TP {{tp|p=26101253|t=2015. Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes |pdf=|usr=}}{{26101253}} gab.com Text Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=26101253 #FOAvip Recent studies showed that Rai1 and its homologs are a crucial component of the mRNA 5?-end capping quality control mechanism. They can possess RNA 5?-end pyrophosphohydrolase (PPH), decapping, and 5?-3? exonuclease (toward 5? monophosphate RNA) activities, which help to degrade mRNAs with incomplete 5?-end capping. A single active site in the enzyme supports these apparently distinct activities. However, each Rai1 protein studied so far has a unique set of activities, and the molecular basis for these differences are not known. Here, we have characterized the highly diverse activity profiles of Rai1 homologs from a collection of fungal organisms and identified a new activity for these enzymes, 5?-end triphosphonucleotide hydrolase (TPH) instead of PPH activity. Crystal structures of two of these enzymes bound to RNA oligonucleotides reveal differences in the RNA binding modes. Structure-based mutations of these enzymes, changing residues that contact the RNA but are poorly conserved, have substantial effects on their activity, providing a framework to begin to understand the molecular basis for the different activity profiles. Twit Text FOAVip Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=26101253 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26101253 #FOAvip English Wikipedia <ref>{{Cite pmid|26101253}}</ref> Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes #MMPMID26101253 Wang VYF; Jiao X; Kiledjian M; Tong L Nucleic Acids Res 2015[Jul]; 43 (13): 6596-606 PMID26101253show ga Recent studies showed that Rai1 and its homologs are a crucial component of the mRNA 5?-end capping quality control mechanism. They can possess RNA 5?-end pyrophosphohydrolase (PPH), decapping, and 5?-3? exonuclease (toward 5? monophosphate RNA) activities, which help to degrade mRNAs with incomplete 5?-end capping. A single active site in the enzyme supports these apparently distinct activities. However, each Rai1 protein studied so far has a unique set of activities, and the molecular basis for these differences are not known. Here, we have characterized the highly diverse activity profiles of Rai1 homologs from a collection of fungal organisms and identified a new activity for these enzymes, 5?-end triphosphonucleotide hydrolase (TPH) instead of PPH activity. Crystal structures of two of these enzymes bound to RNA oligonucleotides reveal differences in the RNA binding modes. Structure-based mutations of these enzymes, changing residues that contact the RNA but are poorly conserved, have substantial effects on their activity, providing a framework to begin to understand the molecular basis for the different activity profiles. äStructural and biochemical studies of the distinct activity profiles o(epmc).pdf DeepDyve Pubget Overpricing