Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances

• Published in: RNA biology Vol. 15; no. 4-5; pp. 480 - 491
• Main Authors: Fields, Rachel N., Roy, Hervé
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 04.05.2018
• Subjects: Amino Acids - genetics; Amino Acids - metabolism; Anti-Bacterial Agents - pharmacology; Antimicrobial Cationic Peptides - pharmacology; antimicrobial resistance; Bacteria - drug effects; Bacteria - genetics; Bacteria - metabolism; Cardiolipins - metabolism; cationic antimicrobial peptides; Cell Membrane - drug effects; Cell Membrane - genetics; Cell Membrane - metabolism; Diglycerides - metabolism; Drug Resistance, Bacterial - genetics; Lipid aminoacylation; Membrane Lipids - metabolism; Phosphatidylglycerols - metabolism; Protein Folding; Review - Solicited; RNA, Transfer - genetics; RNA, Transfer - metabolism; Transfer RNA Aminoacylation; Transferases (Other Substituted Phosphate Groups) - genetics; Transferases (Other Substituted Phosphate Groups) - metabolism; tRNA; Virulence; Lipid aminoacylation; tRNA; antimicrobial resistance; cationic antimicrobial peptides
• ISSN: 1547-6286; 1555-8584
• DOI: 10.1080/15476286.2017.1356980

tRNA-dependent addition of amino acids to lipids on the outer surface of the bacterial membrane results in decreased effectiveness of antimicrobials such as cationic antimicrobial peptides (CAMPs) that target the membrane, and increased virulence of several pathogenic species. After a brief introduction to CAMPs and the various bacterial resistance mechanisms used to counteract these compounds, this review focuses on recent advances in tRNA-dependent pathways for lipid modification in bacteria. Phenotypes associated with amino acid lipid modifications and regulation of their expression will also be discussed.