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 A Nor Muhammad, Stuart G Dashper, Vladimir A Likic, Dhana G Gorasia, Dina Chen, Samantha J Byrne, Deanne V Catmull, Eric C Reynolds
JOURNAL OF PROTEOME RESEARCH | AMER CHEMICAL SOC | Published : 2013
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..View full abstract
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Awarded by Australian National Health and Medical Research Council
This project was supported by the Australian National Health and Medical Research Council Project Grant # 1027812. Ms. Rita Paolini is thanked for technical assistance with bacterial culture.