10.1021/pr400487b.s003
Paul D. Veith
Paul D.
Veith
Nor A. Nor Muhammad
Nor
A. Nor Muhammad
Stuart G. Dashper
Stuart G.
Dashper
Vladimir A. Likić
Vladimir A.
Likić
Dhana G. Gorasia
Dhana G.
Gorasia
Dina Chen
Dina
Chen
Samantha J. Byrne
Samantha J.
Byrne
Deanne V. Catmull
Deanne V.
Catmull
Eric C. Reynolds
Eric C.
Reynolds
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
American Chemical Society
2013
Novel Secretion System
Prevotella intermedia
bioinformatic analyses
Bacteroidetes Phylum
secretion system
Protein Substrates
Porphyromonas gingivalis
CTD cleavage site
Parabacteroides distasonis
Markov Models
HMM
Tannerella forsythia
cleavage site
membrane localization
PG
sequence motifs
Cytophaga hutchinsonii
CTD proteins
Proteomic analyses
culture fluid
Bacteroidetes phylum
cell surface
species
membrane fractions
2013-10-04 00:00:00
Dataset
https://acs.figshare.com/articles/dataset/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/2370730
The secretion of certain proteins
in <i>Porphyromonas gingivalis</i> 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 <i>Bacteroidetes</i> phylum, while no CTD-containing proteins were
predicted in species outside this phylum. Further HMM searching of <i>Cytophaga hutchinsonii</i> led to a total of 171 predicted CTD
proteins in that organism alone. Proteomic analyses of membrane fractions
and culture fluid derived from <i>P. gingivalis</i> and
four other species containing predicted CTDs (<i>Parabacteroides
distasonis</i>, <i>Prevotella intermedia</i>, <i>Tannerella forsythia</i>, and <i>C. hutchinsonii</i>) 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 <i>P. gingivalis</i>, suggesting
that homologues of the C-terminal signal peptidase (PG0026) are responsible
for the cleavage in these species.