Disease relevance of tRNA-Ser

• It binds tRNASer (yeast), tRNAAla (yeast) and tRNATyr (E. coli) with a binding constant about 100 times lower compared to its cognate tRNA [1].

High impact information on tRNA-Ser

• Our results suggest that this may be the only gene for tRNASer in yeast which contains an intervening sequence [2].
• DNA sequence analysis of polymorphic variants of SUQ5, a tRNA Ser UCA gene, and SUP2, a tRNA Tyr gene, shows that in each case one sequence variant of the tRNA gene is 346 base pairs longer than the other [3].
• Differences in the processing of dimeric tRNASer-tRNAMet precursors derived from the Schizosaccharomyces pombe sup9 wild-type and opal suppressor genes can be attributed to conformational alterations in the tRNASer anticodon/intron domain [4].
• Sequence analysis of two yeast mitochondrial DNA fragments containing the genes for tRNA Ser UCR and tRNA Phe UUY [5].
• One of these fragments is 320 base pairs long and contains a tRNA Ser gene [5].

Biological context of tRNA-Ser

• Yeast seryl tRNA synthetase: interactions between the ATP binding site and the sites for tRNASer and L-serine [6].
• Seryl tRNA synthetase from Saccharomyces Carlsbergensis C836 contains two sets of sites for tRNASer, L-serine, and Mg2+-ATP, both of which are involved in aminoacylation [7].
• RNA sequence analysis of this tRNA indicated that the suppressor is derived from a UCA-decoding tRNA Ser by a G leads to U substitution in the middle position of the anticodon [8].
• More surprisingly, extended sequence homologies were seen between the flanking regions of the pY 20 tRNA Glu 3 gene and a tRNA Ser gene [2,3] [9].
• The suppressor mutation was mapped by genetic and molecular analyses in the mitochondrial tRNASer-var1 region of the mitochondrial genome of the yeast S. cerevisiae [10].

Associations of tRNA-Ser with chemical compounds

• The results indicate that under normal conditions, the activity of seryl tRNA synthetase is regulated mainly by tRNASer while at high serine concentrations regulation by the amino acid itself prevails [7].
• The suppressor further differs from the wild-type UCA-decoding tRNA Ser in that the mutant anticodon lacks the modified uridine found in the wobble position of the wild-type tRNA and contains instead another modification in or near the anticodon [8].
• Introducing a set of three base substitutions at positions 35, 37 and 73 was sufficient to convert tRNASer into an efficient leucine acceptor [11].
• By following the tryptophan fluorescence of yeast seryl-tRNA synthetase on addition of tRNA Ser it was observed that the number of binding sites for tRNA decreases from two to one with increasing temperature, ATP or KCl concentration [12].

Other interactions of tRNA-Ser

• In a systematic study of the stoichiometry of protection it was confirmed that under standard conditions one phenylalanyl-tRNA synthetase protects one tRNA-Phe and one seryl-tRNA synthetase two tRNA-Ser molecules against nuclease attack [13].
• Prokaryotes have three amino acid-specific class II tRNAs that possess a characteristic long variable arm, tRNASer, tRNALeuand tRNATyr, while eukaryotes have only two, tRNASerand tRNALeu [14].

References