Mechanism of localization of major outer membrane lipoprotein in Escherichia coli. Studies with the OmpF-lipoprotein hybrid protein.

摘要: A chimera gene consisting of the ompF promoter, coding regions for signal peptide and NH2-terminal 11 amino acid residues outer membrane OmpF protein, region major lipoprotein devoid 7 was constructed. Escherichia coli carrying cloned produced a hybrid protein with predicted chemical structure. The localized in periplasmic space an interaction peptidoglycan layer. These results indicate that expressed, secreted across cytoplasmic membrane, processed normally. however, not incorporated into suggesting importance lipid domain assembly membrane. Although larger part extractable sodium dodecyl sulfate, covalently bound to layer as is. Upon treatment lysozyme envelope became water soluble. solubilized most probably existed trimer. likely suggest exists trimer interactions through on one side other side.