Association of thioredoxin with the inner membrane and adhesion sites in Escherichia coli.

摘要: The intracellular localization of thioredoxin in Escherichia coli was determined by immunoelectron microscopy and correlated to previous biochemical data which had suggested that resides at inner-outer membrane adhesion sites. Since a considerable amount lost during preparation cells for electron microscopy, we immobilized the protein with heterobifunctional photoactivatable cross-linker p-azidophenacylbromide before were fixed aldehyde embedded Lowicryl K4M. Thin sections labeled affinity-purified antithioredoxin antiserum A-gold complexes. Densities immunolabel designated membrane-associated area rest cytoplasm compared statistically evaluated. Wild-type strain W3110 SK3981, an overproducer thioredoxin, exhibited increased labeling inner its adjacent cytoplasmic area. In contrast, more centrally located both strains showed much lower label density. This distribution did not change cell growth or stationary phase. Immunolabel often found bridges between outer membranes; this result is consistent model places least portion sites, corresponding osmotically sensitive compartment bounded hybrid (C.A. Lunn V. Pigiet, J. Biol. Chem. 257:11424-11430, 1982; C.A. 261:832-838, 1986). Specific absent periplasmic space.