I. H. Madshus, H. Stenmark (auth.), Professor Dr. Dr. Klaus's ADP-Ribosylating Toxins PDF

By I. H. Madshus, H. Stenmark (auth.), Professor Dr. Dr. Klaus Aktories (eds.)

ISBN-10: 3642769667

ISBN-13: 9783642769665

ISBN-10: 3642769683

ISBN-13: 9783642769689

ADP-ribosylating pollution were the point of interest of in depth study for greater than 30 years. Researchers from various fields of technological know-how have taken an curiosity in those bacterial pollutants; they're studied, for instance, by way of microbiologists, biochemists, cellphone biologists, and pharmacologists. There are valuable purposes for the huge and nonetheless growing to be curiosity in ADP­ ribosylating pollutants. First, insights into the constitution and services of the pollutants can be the major to prevention and therapy of illnesses because of the toxin-producing infectious micro­ organisms. moment, the ADP-ribosylating pollution offer effective and infrequently designated pharmacological instruments for the learn of the physiological capabilities in their goal proteins. The latter is principally the case with cholera and pertussis pollution, which either regulate the IX-subunits of heterotrimeric G-proteins focused on sign transduction pathways. those pollution have proved necessary in extending our easy realizing of the law of hormone-controlled sign transduction. This quantity presents a overview and an replace of modern experiences at the simple houses of bacterial ADP-ribosylating tbxins and/or exoenzymes. Our present wisdom of the cel­ lular access mechanisms of ADP-ribosylating pollutants is reviewed through MADSHUS and STENMARK. WILSON and COLLIER then take care of contemporary insights into the enzyme mechanism and energetic web site constitution of diphtheria toxin and Pseudomonas aeruginosa exotoxin A, which alter elongation issue 2. pollution which ADP-ribosylate heterotrimeric G-proteins all in favour of trans­ membrane sign transduction are the topic of the subsequent chapters.

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Eur J Biochem 146:503-508 Tamura M, Nogimori K, Yajima M, Ito K, Katada T, Ui M, Ishii S (1982) Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model. Biochemistry 21:5516-5522 Thompson MR, Forristal J, Kauffmann P, Madden T, Kozak K, Morris R, Saelinger CB (1991) Isolation and characterization of Pseudomonas aeruginosa exotoxin A binding glycoprotein from mouse LM cells. J Bioi Chem 266: 2390-2396 Tomasi M, Montecucco C (1981) Lipid insertion of cholera toxin after binding to GM,-containing lipsosomes.

However, it should be reiterated that there is another consistent feature among all these toxins, namely the presence of'a unique, active-site histidine residue, which could conceivably function in conjunction with the carboxyl group to catalyze the AOP-ribosyltransfer reaction. Studies by several research groups are currently in progress to resolve these issues and to address the broader question of the evolutionary relationships among these AOP-ribosyltransferases. 0-Angstrom resolution. Proc Natl Acad Sci USA 83: 1320-1324 Allured YS, Brandhuber BJ, McKay DB (1987) Structure and mechanism of exotoxin A of Pseudomonas aeruginosa.

J Bioi Chem 256: 11177-11181 Tomasi M, Battistini A, Ausiello C, Roda LG, d'Angolo GD (1978) The role of environmental parameters on the stability of cholera toxin functional regions. FEBS Lett 94: 253-256 26 I. H. Madshus and H. Stenmark: Entry of ADP-Ribosylating Toxins into Cells Tosteson MT, Tosteson DC (1978) Bilayers containing gangliosides develop channels when exposed to cholera toxin. Nature 275: 142-144 Tsuji T, Honda T, Miwatani T, Wakabayashi S, Matsubara H (1984) The amino acid sequence of the B-subunit: of porcine enterotoxigenic Escherichia coli enterotoxin- analysis and comparison with literature data.

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ADP-Ribosylating Toxins by I. H. Madshus, H. Stenmark (auth.), Professor Dr. Dr. Klaus Aktories (eds.)

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