TRNA lysidinylation is essential for the minimal translation system found in the apicoplast of <i>Plasmodium falciparum</i>.

ABSTRACT: For decades, researchers have sought to define minimal genomes to elucidate the fundamental principles of life and advance biotechnology. tRNAs, essential components of this machinery, decode mRNA codons into amino acids. The apicoplast of malaria parasites encodes 25 tRNA isotypes in its organellar genome - the lowest number found in known translation systems. Efficient translation in such minimal systems depends heavily on post-transcriptional tRNA modifications, especially at the wobble anticodon position. Lysidine modification at the wobble position (C34) of tRNA_CAU distinguishes between methionine (AUG) and isoleucine (AUA) codons, altering the amino acid delivered by this tRNA and ensuring accurate protein synthesis. Lysidine is formed by the enzyme tRNA isoleucine lysidin

SUBMITTER: Elahi R 

PROVIDER: S-EPMC11419160 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature