Sequence‐independent processing site of the C‐terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis

• DOI: 10.1111/mmi.12319
• Publication Date: 2013-07-04T10:44:31Z
• Authors: Xiao‐Yan Zhou; Jin‐Long Gao; Neil Hunter; Jan Potempa; Ky‐Anh Nguyen
• Keywords: CTD; Cleavage (geology); Furin; Lipid-anchored protein

The Gram-negative periodontal pathogen Porphyromonas gingivalis produces a family of outer membrane-anchored proteases, the gingipains, shown to play an essential role in virulence organism. C-terminal domain (CTD) gingipains and other secreted proteins is known be targeting signal for maturation translocation protein through membrane. CTD subsequently cleaved during secretion process. Multiple alignment various CTDs failed define consensus sequence at putative processing site. Using mutagenesis, we were able show that cleavage site not dependent on specific residue recognition independent local sequence. Interestingly, length junction between adjacent Ig-like subdomain has critical influence post-translational glycan modification protein, whereby insertion additional residues immediately N-terminal results failure release soluble protease into culture medium. Various hypotheses are presented explain these phenomena. Knowledge broader application understanding homologues expressed by bacteria Bacteriodetes phylum.