Evolving specificity of tRNA 3-methyl-cytidine-32 (m3C32) modification: a subset of tRNAsSer requires N6-isopentenylation of A37

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FIGURE 2.
FIGURE 2.

Two sequence homologs for TRM140 in S. pombe. (A) Cartoon showing the general domain architecture of S. cerevisiae TRM140 and the two S. pombe homologs. Position of +1 frame shift in S. cerevisiae gene is indicated as +1 FS, which corresponds to amino acid 301; amino acid numbering is further indicated in panel B. (B) Alignment of the two S. pombe homologs of TRM140 with the S. cerevisiae protein. Only the C-terminal domain of the S. cerevisiae protein (starting from 301) is shown. Asterisks indicate amino acids D466, D547, and the horizontal line indicates the C-terminal 20 amino acids important for catalytic activity of TRM140 (Noma et al. 2011). (C) Phylogenetic tree of trm140+ and trm141+ homologs in different species generated from an alignment created using MUSCLE in Jalview (Edgar 2004; Waterhouse et al. 2009).

This Article

  1. RNA 22: 1400-1410