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10.1093/nar/gkaa446 http://scihub22266oqcxt.onion/10.1093/nar/gkaa446 32453412!7544214!32453412     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 2020 ; 48 (18): 10034-10044 Nephropedia Template TP {{tp|p=32453412|t=2020. Beta class amino methyltransferases from bacteria to humans: evolution and structural consequences |pdf=|usr=}}{{32453412}} gab.com Text Beta class amino methyltransferases from bacteria to humans: evolution and structural consequences JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=32453412 #FOAvip S-adenosyl-l-methionine dependent methyltransferases catalyze methyl transfers onto a wide variety of target molecules, including DNA and RNA. We discuss a family of methyltransferases, those that act on the amino groups of adenine or cytosine in DNA, have conserved motifs in a particular order in their amino acid sequence, and are referred to as class beta MTases. Members of this class include M.EcoGII and M.EcoP15I from Escherichia coli, Caulobacter crescentus cell cycle-regulated DNA methyltransferase (CcrM), the MTA1-MTA9 complex from the ciliate Oxytricha, and the mammalian MettL3-MettL14 complex. These methyltransferases all generate N6-methyladenine in DNA, with some members having activity on single-stranded DNA as well as RNA. The beta class of methyltransferases has a unique multimeric feature, forming either homo- or hetero-dimers, allowing the enzyme to use division of labor between two subunits in terms of substrate recognition and methylation. We suggest that M.EcoGII may represent an ancestral form of these enzymes, as its activity is independent of the nucleic acid type (RNA or DNA), its strandedness (single or double), and its sequence (aside from the target adenine). Twit Text FOAVip Beta class amino methyltransferases from bacteria to humans: evolution and structural consequences ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=32453412 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32453412 #FOAvip English Wikipedia <ref>{{Cite pmid|32453412}}</ref> Beta class amino methyltransferases from bacteria to humans: evolution and structural consequences #MMPMID32453412 Woodcock CB; Horton JR; Zhang X; Blumenthal RM; Cheng X Nucleic Acids Res 2020[Oct]; 48 (18): 10034-10044 PMID32453412show ga S-adenosyl-l-methionine dependent methyltransferases catalyze methyl transfers onto a wide variety of target molecules, including DNA and RNA. We discuss a family of methyltransferases, those that act on the amino groups of adenine or cytosine in DNA, have conserved motifs in a particular order in their amino acid sequence, and are referred to as class beta MTases. Members of this class include M.EcoGII and M.EcoP15I from Escherichia coli, Caulobacter crescentus cell cycle-regulated DNA methyltransferase (CcrM), the MTA1-MTA9 complex from the ciliate Oxytricha, and the mammalian MettL3-MettL14 complex. These methyltransferases all generate N6-methyladenine in DNA, with some members having activity on single-stranded DNA as well as RNA. The beta class of methyltransferases has a unique multimeric feature, forming either homo- or hetero-dimers, allowing the enzyme to use division of labor between two subunits in terms of substrate recognition and methylation. We suggest that M.EcoGII may represent an ancestral form of these enzymes, as its activity is independent of the nucleic acid type (RNA or DNA), its strandedness (single or double), and its sequence (aside from the target adenine). |*Evolution, Molecular[MESH] |Amino Acid Sequence[MESH] |Animals[MESH] |Caenorhabditis elegans/enzymology[MESH] |Caulobacter crescentus/enzymology[MESH] |Escherichia coli/enzymology[MESH] |Humans[MESH] |Methyltransferases/*chemistry/classification[MESH] |Mice[MESH] |Oxytricha/enzymology[MESH] |Protein Conformation[MESH]Beta class amino methyltransferases from bacteria to humans: evolution(epmc).pdf DeepDyve Pubget Overpricing