Open AccessPost‐translational processing of Neisseria meningitidis γ‐glutamyl aminopeptidase and its association with inner membrane facing to the cytoplasmic space
Author(s) -
Takahashi Hideyuki,
Watanabe Haruo
Publication year - 2004
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2004.tb09509.x
Subject(s) - neisseria meningitidis , cytoplasm , aminopeptidase , association (psychology) , microbiology and biotechnology , chemistry , biology , bacteria , biochemistry , genetics , amino acid , leucine , psychology , psychotherapist
We previously demonstrated that γ‐glutamyl aminopeptidase (also called γ‐glutamyl transpeptidase) (GGT) of Neisseria meningitidis is involved in the bacterial multiplication in cerebrospinal fluid. To further understand the function of meningococcal GGT, the biochemical properties were investigated in this study. The deduced amino acid sequence in N. meningitidis GGT was 37% identical to that of Escherichia coli GGT and that of Helicobacter pylori GGT, respectively, while a typical signal sequence was not found at the N‐terminus of meningococcal GGT. Western blotting using rabbit antiserum against recombinant meningococcal GGT protein demonstrated that the meningococcal GGT is processed into two subunits in N. meningitidis at the conserved amino acid, threonine 427. The experiments on subcellular fractionation suggested that the majority of meningococcal GGT is associated with inner membrane facing to the cytoplasmic side. This cell localization might be unique for N. meningitidis compared to other GGTs.