Synthetic mycolates derivatives to decipher protein mycoloylation, a unique post-translational modification in bacteria.
Ontology highlight
ABSTRACT: Protein mycoloylation is a newly characterized post-translational modification (PTM) specifically found in Corynebacteriales, an order of bacteria that includes numerous human pathogens. Their envelope is composed of a unique outer membrane, the so-called mycomembrane made of very-long chain fatty acids, named mycolic acids. Recently, some mycomembrane proteins including PorA have been unambiguously shown to be covalently modified with mycolic acids in the model organism Corynebacterium glutamicum by a mechanism that relies on the mycoloyltransferase MytC. This PTM represents the first example of protein O-acylation in prokaryotes and the first example of protein modification by mycolic acid. Through the design and synthesis of trehalose monomycolate (TMM) analogs, we prove that i) MytC is
SUBMITTER: Lesur E
PROVIDER: S-EPMC11927696 | biostudies-literature | 2025 Mar
REPOSITORIES: biostudies-literature
ACCESS DATA