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..com/assets/c2/60/cc/84/00/Ghost_In_The_Shell_1995_Torrent.html. -fixed-cambridge-english-proficiency-practice-tests-pdf-download . Category:Ghost in the ShellEnergy-driven biosynthesis and metabolism of a novel inosine cap methylated nucleoside analogue in the hyperthermophilic archaeon Thermococcus zilligii. 1-Methylinosine (m(1)I) is a special structural element of bacterial and archaeal genomes where it replaces adenine and guanine in codon positions 1 and 2. This chemical modification in the second DNA codon position can induce translational errors and thus reduce protein expression. The single inosine residue m(1)I is however also a metabolite of some bacteria and archaea. Yet, in most of these species, the m(1)I is synthesized in a two-step pathway via 5-methyluridine, whereas in hyperthermophilic archaea, including the model organism Thermococcus zilligii, it is only formed by one enzymatic step. Here we show that T. zilligii contains an inosine cap methyltransferase (Tzil1) which is specific for the m(1)I. This protein has an S-adenosyl-l-methionine binding site, and is able to methylate RNA substrates at the N(6)-position. The N(7)-O(6)-position of inosine can be methylated via a cooperative formation of a tyrosine and histidine residue. Besides inosine and m(1)I, T. zilligii further possesses adenosine, guanosine, 5-methyluridine, pseudouridine and 5-methylcytidine. Our results identify T. zilligii as the first prokaryotic organism where both, the m(1)I and the energy-dependent two-step pathway for its synthesis, are present. Furthermore, we show that the two pathways are employed in the same time for the synthesis of m(1)I. The isolation of hyperthermophilic archaeal organisms is an important step to identify their own type of energy-dependent inosine synthesis. We therefore conclude that archaeal m(1)I is predominantly synthetized

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