The tRNA structure contains conserved modifications that are responsible for its stability and are involved in the initiation and accuracy of the translation process. tRNA modification enzymes are prevalent in bacteria, archaea, and eukaryotes. tRNA Gm18 methyltransferase (TrmH) and tRNA m(1)G37 methyltransferase (TrmD) are prevalent and essential enzymes in bacterial populations. TrmH involves itself in methylation process at the 2'-OH group of ribose at the 18th position of guanosine (G) in tRNAs. TrmD methylates the G residue next to the anticodon in selected tRNA subsets. Initially, m(1)G37 modification was reported to take place on three conserved tRNA subsets (tRNA(Arg), tRNA(Leu), tRNA(Pro)); later on, few archaea and eukaryotes organisms revealed that other tRNAs also have the m(1)G37 modification. The present study reveals Gm18, m(1)G37 modification, and positions of m(1)G that take place next to the anticodon in tRNA sequences. We selected extremophile organisms and attempted to retrieve the m(1)G and Gm18 modification bases in tRNA sequences. Results showed that the Gm18 modification G residue occurs in all tRNA subsets except three tRNAs (tRNA(Met), tRNA(Pro), tRNA(Val)). Whereas the m(1)G37 modification base G is formed only on tRNA(Arg), tRNA(Leu), tRNA(Pro), and tRNA(His), the rest of the tRNAs contain adenine (A) next to the anticodon. Thus, we hypothesize that Gm18 modification and m(1)G modification occur irrespective of a G residue in tRNAs.
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| http://dx.doi.org/10.5808/GI.2014.12.2.71 | DOI Listing |
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