Deciphering The Trna-Dependent Lipid Aminoacylation Systems In Bacteria: Novel Components And Structural Advances
Keywords
antimicrobial resistance; cationic antimicrobial peptides; Lipid aminoacylation; tRNA
Abstract
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.
Publication Date
5-4-2018
Publication Title
RNA Biology
Volume
15
Issue
4-5
Number of Pages
480-491
Document Type
Article
Personal Identifier
scopus
DOI Link
https://doi.org/10.1080/15476286.2017.1356980
Copyright Status
Unknown
Socpus ID
85044608422 (Scopus)
Source API URL
https://api.elsevier.com/content/abstract/scopus_id/85044608422
STARS Citation
Fields, Rachel N. and Roy, Hervé, "Deciphering The Trna-Dependent Lipid Aminoacylation Systems In Bacteria: Novel Components And Structural Advances" (2018). Scopus Export 2015-2019. 10185.
https://stars.library.ucf.edu/scopus2015/10185