ArticlePloS one2017
Click-chemistry approach to study mycoloylated proteins: Evidence for PorB and PorC porins mycoloylation in Corynebacterium glutamicum.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 26 citations in OpenAlex.
- The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Metabolic Tagging Reveals Surface-Associated Lipoproteins in Mycobacteria.ACS infectious diseases · 2025Article
- Metabolic tagging reveals surface-associated lipoproteins in mycobacteria.bioRxiv : the preprint server for biology · 2025Article
- Synthetic Lipid Biology.Chemical reviews · 2025Review
- The conserved σD envelope stress response monitors multiple aspects of envelope integrity in corynebacteria.PLoS genetics · 2024Article
- Chemical Proteomics Strategies for Analyzing Protein Lipidation Reveal the BacterialJournal of the American Chemical Society · 2024Article
- Article
- Application of Corynebacterium glutamicum engineering display system in three generations of biorefinery.Microbial cell factories · 2022Review
- Genome-Scale Mining of Novel Anchor Proteins ofFrontiers in microbiology · 2021Article
- Engineering the Mycomembrane of Live Mycobacteria with an Expanded Set of Trehalose Monomycolate Analogues.Chembiochem : a European journal of chemical biology · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein mycoloylation is a recently identified, new form of protein acylation. This post-translational modification consists in the covalent attachment of mycolic acids residues to serine. Mycolic acids are long chain, α-branched, β-hydroxylated fatty acids that are exclusively found in the cell envelope of Corynebacteriales, a bacterial order that includes important genera such as Mycobacterium, Nocardia or Corynebacterium. So far, only 3 mycoloylated proteins have been identified: PorA, PorH and ProtX from C. glutamicum. Whereas the identity and function of ProtX is unknown, PorH and PorA associate to form a membrane channel, the activity of which is dependent upon PorA mycoloylation. However, the exact role of mycoloylation and the generality of this phenomenon are still unknown. In particular, the identity of other mycoloylated proteins, if any, needs to be determined together with establishing whether such modification occurs in Corynebacteriales genera other than Corynebacterium. Here, we tested whether a metabolic labeling and click-chemistry approach could be used to detect mycoloylated proteins. Using a fatty acid alkyne analogue, we could indeed label PorA, PorH and ProtX and determine ProtX mycoloylation site. Importantly, we also show that two other porins from C. glutamicum, PorB and PorC are mycoloylated.
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