Enterobactin synthase polypeptides of Escherichia coli are present in an osmotic-shock-sensitive cytoplasmic locality
Article Abstract:
Electrophoresis, Western blotting, Ent synthase assays, phenolate and protein assays and radioimmune precipitations were done to investigate the the localization and association of the enterobactin (Ent) synthase. Ent synthase, a product of the terminal reactions in the synthesis of the siderophore Ent by Escherichia coli which involve the EntD, E, F and B/G polypeptides, was found to interact with the cellular membrane in vivo. This indicate that the EntE, F and B/G are compartmentalized in the coliform bacteria and since other biosynthetic enzymes for siderophores and surfactants are associated with these Ent proteins, it appears that such class of proteins may be sequestered in vivo.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Topological analysis of the lysine-specific permease of Escherichia coli
Article Abstract:
Several systems exist to transport the basic amino acids arginine, lysine and ornithine in Escherichia coli. There are two systems, one specific for lysine (LysP) and another inhibited by arginine or ornithine (LAO), through which Escherichia coli stores lysin. A topological model of LysP proposes a 12 membrane-spanning alpha-helices joined by six periplasmic loops and five cytoplasmic loops. The N- and C-termini could be cytosolic and exact position of each residue could not be known from the data.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
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