Suppressors of lysine codons may be misacylated lysine tRNAs

Suppressors of lysine codons may be misacylated lysine tRNAs.

We describe a novel class of missense suppressors that read the codons for lysine at two positions (211 and 234) in the trpA polypeptide of Escherichia coli. The suppressor mutations are highly linked to lysT, a gene for lysine tRNA. The results suggest that the suppressors are misacylated lysine tRNAs that carry glycine or alanine. The mutant codons are apparently suppressed better at position...

Lysine tRNAs from rat liver: lysine tRNA sequences are highly conserved.

The two major lysine tRNAs from rat liver, tRNA2Lys and tRNA5Lys, were sequenced by rapid gel or chromatogram readout methods. The major tRNA2Lys differs from a minor form only by a base pair in positions 29 and 41; both tRNAs have an unidentified nucleotide, U**, in the third position of the anticodon. Although highly related, the major tRNA2Lys and tRNA5Lys differ in four base pairs and four ...

Lysine tRNAs from Bacillus subtilis 168: structural analysis.

The primary sequence was established for two lysine tRNA isoacceptors which differ in abundance during development in Bacillus subtilis. Both tRNAs shared the same primary sequence but differed in the degree of post-transcriptional modification in the anticodon loop. The earlier eluting species, tRNA lys 1, had an unmodified C in position 32 and a mixture of N-[9-beta-ribofuranosyl) purin-6-ylc...

Strictly Conserved Lysine of Prolyl-tRNA Synthetase Editing Domain Facilitates Binding and Positioning of Misacylated tRNAPro

To ensure high fidelity in translation, many aminoacyl-tRNA synthetases, enzymes responsible for attaching specific amino acids to cognate tRNAs, require proof-reading mechanisms. Most bacterial prolyl-tRNA synthetases (ProRSs) misactivate alanine and employ a post-transfer editing mechanism to hydrolyze Ala-tRNA(Pro). This reaction occurs in a second catalytic site (INS) that is distinct from ...

Fragmentation Studies of Lysine and Lysine Analog Containing Tetrapeptides