Identification of specific posttranslational O -mycoloylations mediating protein targeting to the mycomembrane
Open accessAbstract
Significance: Protein secretion is an essential determinant of bacterial physiology and virulence. Members of the Corynebacteriales order have evolved a complex cell envelope containing two membranes, a plasma membrane and an outer membrane, called the mycomembrane, which harbors mycolic acids and outer membrane proteins (OMPs) of unusual structure. Here, we have investigated the biogenesis of OMPs in Corynebacterium glutamicum and deciphered the role of O -mycoloylation in targeting OMPs to the mycomembrane. Partially enabled by our methodology, we found that the posttranslational state of major OMPs determined their presence in the outer membrane vs. the extracellular medium. We have also uncovered a short linear amino acid motif for O -acylation of proteins that seems to be preserved throughout the kingdoms.
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Within the field of infectious diseases, proteoform-resolved approaches have been instrumental for understanding infectivity and dissemination of Salmonella typhimurium, Corynebacterium glutamicum and Neisseria meningitidis.
“Within the field of infectious diseases, proteoform-resolved approaches have been instrumental for understanding infectivity and dissemination of Salmonella typhimurium 67 , Corynebacterium glutamicum 68 and Neisseria meningitidis 69 .”
From How many human proteoforms are there? (2018) · cites this paper as [68]
For the Corynebacterium glutamicum portion of the sentence, the Discussion (p. 5) describes top-down mass spectrometry identifying distinct proteoforms, and the Significance section (p. 1) links their posttranslational state to outer-membrane targeting versus secretion. The paper does not establish effects on infectivity or bacterial dissemination; it studies protein localization in C. glutamicum. (LLM, conf=0.88)
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Cites
The lipocalin protein family: structural and sequence overview
Flower, D. R., North, A. C. T., & Sansom, C. E. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00148-5 · Cited by 868 · see citing works
Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J. M., & Engelhardt, H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709530105 · Cited by 596 · see citing works
Decoding protein modifications using top-down mass spectrometry
Siuti, N., & Kelleher, N. L. (2007) · Nature Methods · doi:10.1038/nmeth1097 · Cited by 503 · see citing works
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How many human proteoforms are there?
Aebersold, R., Agar, J. N., Amster, I. J., Baker, M. S., Bertozzi, C. R., Boja, E. S., Costello, C. E., Cravatt, B. F., Fenselau, C., Garcia, B. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2576 · Cited by 907 · see citing works
Top-Down Proteomics: Ready for Prime Time?
Chen, B., Brown, K. A., Lin, Z., & Ge, Y. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04747 · Cited by 210 · see citing works
Tucholski, T., Knott, S. J., Chen, B., Pistono, P., Lin, Z., & Ge, Y. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04082 · Cited by 49 · see citing works
- Authors
- Carel, C., Marcoux, J., Réat, V., Parra, J., Latgé, G., Laval, F., Demange, P., Burlet-Schiltz, O., Milon, A., Daffé, M., Tropis, M. G., & Renault, M. A. M.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, Université Paul Sabatier, 31000 Toulouse, France
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-04-03
- Volume
- 114
- Issue
- 16
- Pages
- 4231-4236
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5402430
- OpenAlex
- W2604402597
- Cited by
- 36
- References
- 3
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 8 · 2023: 2 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 4 · 2018: 4 · 2017: 2
- FWCI
- 2.54
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ORBi (University of Liège) (submittedVersion, other-oa)
- HAL (submittedVersion)
- Funders
- Agence Nationale de la Recherche (ANR-13-JSV8-0001-01)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Diphtheria, Corynebacterium, and Tetanus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- post-translational modification, outer membrane proteins, mycomembrane, protein targeting, Corynebacterium glutamicum, Corynebacteriales, mycolic acids, outer membrane biogenesis, bacterial cell envelope, protein secretion
- MeSH terms
- Amino Acid Sequence, Bacterial Outer Membrane Proteins, Cell Membrane, Cell Wall, Lipid Bilayers, Mycolic Acids, Protein Processing, Post-Translational, Sequence Homology, Protein Transport, Corynebacterium glutamicum
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