Organization of Diphtheria Toxin in Membranes
نویسندگان
چکیده
منابع مشابه
Diphtheria Toxin In
Recent studies have demonstrated that diphtheria toxin is an enzyme of unusual type. Small amounts of the toxin, added to nicotinamide adenine dinucleotide (NAD)-containing mammalian cell extracts, block peptide-bond formation by catalyzing inactivation of the translocating enzyme, aminoacyltransferase 2 (T2) (1-3). This highly specific reaction involves the splitting of NAD with liberation of ...
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Toxin of sufficient strength to kill a 400-gramme guinea-pig in three days and a half in a dose of 0.cubic centimetre developed in suitable bouillon, contained in ordinary Erlenmeyer flasks, within a period of twenty-four hours. In such boullon the toxin reached its greatest strength in from four to seven days (0.005 cubic centimetre killing a 500-gramme guinea-pig in three days). This period o...
متن کاملLigand Interactions of Diphtheria Toxin
Prior studies have described two functionally distinct ligand-binding sites on whole diphtheria toxin, the NAD site, which catalyzes the intracellular ADP-ribosylation reaction, and the P site, which affects toxin binding to sensitive cells. Occupancy of the P site by ATP or other phosphorylated compounds inhibits toxin attachment to cells. Here we show that binding of NAD site and P site ligan...
متن کاملIdentification of diphtheria toxin receptor and a nonproteinous diphtheria toxin-binding molecule in Vero cell membrane
Two substances possessing the ability to bind to diphtheria toxin (DT) were found to be present in a membrane fraction from DT-sensitive Vero cells. One of these substances was found on the basis of its ability to bind DT and inhibit its cytotoxic effect. This inhibitory substance competitively inhibited the binding of DT to Vero cells. However this inhibitor could not bind to CRM197, the produ...
متن کاملPrecursor in cotranslational secretion of diphtheria toxin.
By extracellular labeling of peptides of intact Corynebacterium diphtheriae, followed by fractionation of the cells and chain completion by isolated polysomes, it is shown that diphtheria toxin is formed and secreted cotranslationally by membrane-bound polysomes; free polysomes from none. Moreover, when the chains on these polysomes were completed in vitro, in the absence of membrane they were ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.275.16.11771