Mass Spectrometry Analysis of the Extracellular Peptidome of Lactococcus lactis: Lines of Evidence for the Coexistence of Extracellular Protein Hydrolysis and Intracellular Peptide Excretion
| Autor: | Véronique Monnet, Emilie Chambellon, Christophe Gitton, Mylène Boulay, Vincent Juillard, Alain Guillot |
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| Přispěvatelé: | MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Proteomics Proteases Cytoplasm substrate specificity Proteolysis medicine.medical_treatment [SDV]Life Sciences [q-bio] Peptide Biology Biochemistry Mass Spectrometry 03 medical and health sciences cell surface proteolysis Bacterial Proteins medicine Extracellular extracellular cytoplasmic peptide chemistry.chemical_classification Protease medicine.diagnostic_test Lactococcus lactis Cell Membrane Serine Endopeptidases peptidomics General Chemistry biology.organism_classification Endopeptidase Amino acid 030104 developmental biology chemistry cell lysis Peptides Amino Acids Branched-Chain Peptide Hydrolases |
| Zdroj: | Journal of Proteome Research Journal of Proteome Research, American Chemical Society, 2016, 15 (9), pp.3214-3224. ⟨10.1021/acs.jproteome.6b00424⟩ |
| ISSN: | 1535-3907 1535-3893 |
| Popis: | We report here the use of a peptidomic approach to revisit the extracellular proteolysis of Lactococcus lactis. More than 1800 distinct peptides accumulate externally during growth of the plasmid-free protease-negative strain L. lactis IL1403 in a protein- and peptide-free medium. These peptides mainly originate from cell-surface- and cytoplasmic located proteins, despite the fact that no cell lysis could be evidenced. Positioning each identified peptide on its parental protein sequence demonstrated the involvement of exo- and endopeptidase activities. The endopeptidases responsible for the release of surface and cytoplasmic peptides had distinct specificities. The membrane-anchored protease HtrA was responsible for the release of only a part of the surface peptides, and its preference for branched-chain amino acids in the N-terminal side of the cleaved bond was established in situ. Other yet uncharacterized surface proteases were also involved. Several lines of evidence suggest that surface and cytoplasmic peptides were produced by different routes, at least part of the latter being most likely excreted as peptides from the cells. The mechanism by which these cytoplasmic peptides are excreted remains an open question, as it is still the case for excreted cytoplasmic proteins. |
| Databáze: | OpenAIRE |
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