ArticleMolecular microbiology2015
tRNA-dependent alanylation of diacylglycerol and phosphatidylglycerol in Corynebacterium glutamicum.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Cryo-EM structures of multiple-peptide resistance factor (MprF) from Pseudomonas aeruginosa.The FEBS journal · 2026Article
- Mapping unsolved lipidomes accelerates lipid discovery in major bacterial pathogens.bioRxiv : the preprint server for biology · 2025Article
- The MprF homolog LysX synthesizes lysyl-diacylglycerol contributing to antibiotic resistance and virulence.Microbiology spectrum · 2023Article
- Construction of a Bacterial Lipidomics Analytical Platform: Pilot Validation with Bovine Paratuberculosis Serum.Metabolites · 2023Article
- RNA-dependent sterol aspartylation in fungi.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Deciphering the tRNA-dependent lipid aminoacylation systems in bacteria: Novel components and structural advances.RNA biology · 2018Review
- A Quantitative Spectrophotometric Assay to Monitor the tRNA-Dependent Pathway for Lipid Aminoacylation In Vitro.Journal of biomolecular screening · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Aminoacyl-phosphatidylglycerol synthases (aaPGSs) are membrane proteins that utilize aminoacylated tRNAs to modify membrane lipids with amino acids. Aminoacylation of membrane lipids alters the biochemical properties of the cytoplasmic membrane and enables bacteria to adapt to changes in environmental conditions. aaPGSs utilize alanine, lysine and arginine as modifying amino acids, and the primary lipid recipients have heretofore been defined as phosphatidylglycerol (PG) and cardiolipin. Here we identify a new pathway for lipid aminoacylation, conserved in many Actinobacteria, which results in formation of Ala-PG and a novel alanylated lipid, Alanyl-diacylglycerol (Ala-DAG). Ala-DAG formation in Corynebacterium glutamicum is dependent on the activity of an aaPGS homolog, whereas formation of Ala-PG requires the same enzyme acting in concert with a putative esterase encoded upstream. The presence of alanylated lipids is sufficient to enhance the bacterial fitness of C. glutamicum cultured in the presence of certain antimicrobial agents, and elucidation of this system expands the known repertoire of membrane lipids acting as substrates for amino acid modification in bacterial cells.
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Registered trials
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