Related Experiment Video
Updated: Jun 12, 2026

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
Published on: May 21, 2018
O-mycoloylated proteins from Corynebacterium: an unprecedented post-translational modification in bacteria
Emilie Huc1, Xavier Meniche, Roland Benz
1Centre National de la Recherche Scientifique, Département Mécanismes Moléculaires des Infections Mycobactériennes, Institut de Pharmacologie et de Biologie Structurale, 205 route de Narbonne, F-31077 Toulouse Cedex 04, France.
Abstract:
O-acylation of proteins was known only in a few eukaryotic proteins but never in bacteria. We demonstrate, using a combination of protein chemistry and mass spectrometry, the occurrence of three O-acylated polypeptides in Corynebacterium glutamicum, PorA, PorH, and an unknown small protein. The three polypeptides are O-substituted by mycolic acids, long chain alpha-alkyl and beta-hydroxy fatty acids specifically produced by members of the Corynebacterineae suborder. To date these acids were described only as esterifying trehalose and arabinogalactan, and less frequently glycerol, important components of the highly impermeable outer barrier of Corynebacterineae. We show that the post-translational mycoloylation of PorA occurs at Ser-15 and is necessary for the pore-forming activity of C. glutamicum.
Related Concept Videos
Bacterial Phylum Actinobacteria
Bacterial Protein Maturation
Cytoskeletal Proteins in Bacteria
Gram-negative Bacterial Protein Secretion Systems
Biosynthesis in Bacteria
Coordination of Gene Expression Processes in Bacteria

