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. 2001 Jan 15;20(1-2):231-9.
doi: 10.1093/emboj/20.1.231.

A primordial tRNA modification required for the evolution of life?

G R Björk  1 , K Jacobsson, K Nilsson, M J Johansson, A S Byström, O P Persson
Affiliations

A primordial tRNA modification required for the evolution of life?

G R Björk et al. EMBO J. .

Abstract

The evolution of reading frame maintenance must have been an early event, and presumably preceded the emergence of the three domains Archaea, Bacteria and Eukarya. Features evolved early in reading frame maintenance may still exist in present-day organisms. We show that one such feature may be the modified nucleoside 1-methylguanosine (m(1)G37), which prevents frameshifting and is present adjacent to and 3' of the anticodon (position 37) in the same subset of tRNAs from all organisms, including that with the smallest sequenced genome (Mycoplasma genitalium), and organelles. We have identified the genes encoding the enzyme tRNA(m(1)G37)methyltransferase from all three domains. We also show that they are orthologues, and suggest that they originated from a primordial gene. Lack of m(1)G37 severely impairs the growth of a bacterium and a eukaryote to a similar degree. Yeast tRNA(m(1)G37)methyltransferase also synthesizes 1-methylinosine and participates in the formation of the Y-base (yW). Our results suggest that m(1)G37 existed in tRNA before the divergence of the three domains, and that a tRNA(m(1)G37)methyltrans ferase is part of the minimal set of gene products required for life.

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Figures

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Fig. 1. Growth of the S.cerevisiae congenic pairs TRM5 and trm5::HIS3, and TRM5 and trm5::kanMX4 (see key to strain at the bottom of the figure) on rich plates after 2 and 9 days, respectively, of incubation at 30°C. After 2 days of incubation, there were no visible colonies of the trm5 mutant.
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Fig. 2. Analysis of modified tRNA nucleosides from wild-type S.cerevisiae TRM5 (upper panel) and the trm5::HIS3 mutant (lower panel). Only the portion of the chromatogram between retention times 47 and 82 min is shown. Abbreviations: t6A, N6-threonylcarbamoyladenosine; Ar, 2′-O-ribosyladenosine; m6A, N6-methyladenosine; yW, wybutosine (nucleoside of the Y-base); i6A, N6-isopentenyladenosine.
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Fig. 3. Sequence of trmD orthologues from E.coli, Aquifex aeolicus, M.jannaschii, S.cerevisiae (yeast), C.elegans and human. The trmD orthologues of C.elegans, A.aeolicus and human were identified by sequence similarities. White letters on a black background indicate similar amino acids in all six species, and white letters on a grey background indicate similar amino acids in at least half of the species. A phylogenetic analysis based on several orthologues of each phylogenic domain revealed that the trmD orthologues fell into the respective domains in a manner typical of macromolecular synthesis of proteins. Numbers above the E.coli sequence are allele numbers for those seven trmD mutations that are located within blocks I or II.
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References

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