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As adaptor molecules linking the codons in a mRNA to the amino acids that they specify, aminoacyl-tRNAs (AA-tRNAs) play a central role in protein biosynthesis. In addition to this critical role, AA-tRNAs are also involved in several other less well known but still important biochemical reactions (Fig. 1). For example, AA-tRNAs are used as substrates for transfer of a single amino acid to the N termini of proteins in a reaction catalyzed by the AA-tRNA-protein transferases (1, 2). The newly attached N-terminal amino acid then acts as a signal for degradation of the protein (3). In another example, the amino acid attached to the tRNA is reduced; glutamyl-tRNA reductase (4) converts the glutamyl residue of glutamyl-tRNA to glutamate 1-semialdehyde, the first precursor in the C5-pathway of porphyrin biosynthesis (5). Two other important uses of AA-tRNA that affect the properties of the cell envelope are (i) the aminoacylation of phospholipids in the cell membrane and (ii) the crosslinking of the peptidoglycan in the cell walls of Gram-positive pathogens. Two recent papers (6, 7), including the one by Roy and Ibba in a recent issue of PNAS (6), focus on these last two reactions by highlighting the role of AA-tRNA in the biosynthesis of the bacterial cell envelope that affects how the cell interacts with antibiotics and antimicrobial peptides. Cellular processes that use AA-tRNA. The individual processes are shown in green, the enzymes/carrier proteins are shown in blue, and some relevant genes are shown in red. The presence of a variety of aminoacyl-phosphatidylglycerol (AA-PG) compounds in bacteria was first described over four decades ago (8). The amino acids identified included lysine, alanine, arginine, and ornithine. Cell-free studies on the enzymes involved in the synthesis of these various AA-PG compounds led to the discovery that lysyl-tRNA is the donor …

Aminoacyl-tRNAs, the bacterial cell envelope, and antibiotics