Protein substrates of a novel secretion system are numerous in the Bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment

Paul D. Veith, Nor Muhammad Nor Azlan, Stuart G. Dashper, Vladimir A. Likić, Dhana G. Gorasia, Dina Chen, Samantha J. Byrne, Deanne V. Catmull, Eric C. Reynolds

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

The secretion of certain proteins in Porphyromonas gingivalis is dependent on a C-terminal domain (CTD). After secretion, the CTD is cleaved prior to extensive modification of the mature protein, probably with lipopolysaccharide, therefore enabling attachment to the cell surface. In this study, bioinformatic analyses of the CTD demonstrated the presence of three conserved sequence motifs. These motifs were used to construct Hidden Markov Models (HMMs) that predicted 663 CTD-containing proteins in 21 fully sequenced species of the Bacteroidetes phylum, while no CTD-containing proteins were predicted in species outside this phylum. Further HMM searching of Cytophaga hutchinsonii led to a total of 171 predicted CTD proteins in that organism alone. Proteomic analyses of membrane fractions and culture fluid derived from P. gingivalis and four other species containing predicted CTDs (Parabacteroides distasonis, Prevotella intermedia, Tannerella forsythia, and C. hutchinsonii) demonstrated that membrane localization, extensive post-translational modification, and CTD-cleavage were conserved features of the secretion system. The CTD cleavage site of 10 different proteins from 3 different species was determined and found to be similar to the cleavage site previously determined in P. gingivalis, suggesting that homologues of the C-terminal signal peptidase (PG0026) are responsible for the cleavage in these species.

Original languageEnglish
Pages (from-to)4449-4461
Number of pages13
JournalJournal of Proteome Research
Volume12
Issue number10
DOIs
Publication statusPublished - 4 Oct 2013
Externally publishedYes

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Bacteroidetes
Porphyromonas gingivalis
Post Translational Protein Processing
Substrates
Cytophaga
Prevotella intermedia
Proteins
Membranes
Conserved Sequence
Hidden Markov models
Computational Biology
Proteomics
Lipopolysaccharides
Bioinformatics
Protein Domains
Fluids

Keywords

  • Bacteroidetes
  • C-terminal signal peptidase
  • novel protein secretion system

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

Cite this

Protein substrates of a novel secretion system are numerous in the Bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment. / Veith, Paul D.; Nor Azlan, Nor Muhammad; Dashper, Stuart G.; Likić, Vladimir A.; Gorasia, Dhana G.; Chen, Dina; Byrne, Samantha J.; Catmull, Deanne V.; Reynolds, Eric C.

In: Journal of Proteome Research, Vol. 12, No. 10, 04.10.2013, p. 4449-4461.

Research output: Contribution to journalArticle

Veith, Paul D. ; Nor Azlan, Nor Muhammad ; Dashper, Stuart G. ; Likić, Vladimir A. ; Gorasia, Dhana G. ; Chen, Dina ; Byrne, Samantha J. ; Catmull, Deanne V. ; Reynolds, Eric C. / Protein substrates of a novel secretion system are numerous in the Bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment. In: Journal of Proteome Research. 2013 ; Vol. 12, No. 10. pp. 4449-4461.
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