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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 pollutants were the focal point of in depth examine for greater than 30 years. Researchers from diversified fields of technological know-how have taken an curiosity in those bacterial pollution; they're studied, for instance, by way of microbiologists, biochemists, phone biologists, and pharmacologists. There are imperative purposes for the extensive and nonetheless becoming curiosity in ADP­ ribosylating pollutants. First, insights into the constitution and capabilities of the pollution will be the foremost to prevention and remedy of ailments attributable to the toxin-producing infectious micro­ organisms. moment, the ADP-ribosylating pollution supply powerful and sometimes exact pharmacological instruments for the learn of the physiological features in their objective proteins. The latter is mainly the case with cholera and pertussis pollution, which either regulate the IX-subunits of heterotrimeric G-proteins inquisitive about sign transduction pathways. those pollutants have proved precious in extending our easy figuring out of the law of hormone-controlled sign transduction. This quantity offers a evaluation and an replace of modern reviews at the simple homes of bacterial ADP-ribosylating tbxins and/or exoenzymes. Our present wisdom of the cel­ lular access mechanisms of ADP-ribosylating pollutants is reviewed by means of MADSHUS and STENMARK. WILSON and COLLIER then care for fresh insights into the enzyme mechanism and energetic website constitution of diphtheria toxin and Pseudomonas aeruginosa exotoxin A, which adjust elongation issue 2. pollutants which ADP-ribosylate heterotrimeric G-proteins occupied with trans­ membrane sign transduction are the topic of the following chapters.

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Extra resources for ADP-Ribosylating Toxins

Example text

When aspartic acid or serine was substituted for Glu-148 in the cloned F2 fragment of DT in Escherichia coli, the ADP-ribosyltransferase activity of the derived mutant fragment A in crude extracts was found to be less than 1 % that of wild-type DTA (TWETEN et al. 1985; BARBIERI and COLLIER 1987). Each mutation produced no alteration in protein stability as measured by protease sensitivity or immunoreactivity, and there was negligible reduction in affinity for NAD. Additionally, the cloned, whole mutant DT, containing the serine substitution at position 148, was found to exhibit an 800-fold decrease in cytotoxicity for cultured B8-C-1 cells (African green monkey kidney cells), a level commensurate with the reduction in ADP-ribosyltransferase activity.

The retention of substrate affinities implied that the mutations did not result in major distortions of the overall protein conformation and that the major effects of the mutations were confined to k eat . Even relatively conservative changes, such as withdrawal of the carboxyl group at position 148 by one methylene unit, as in the aspartate mutant, or replacement of the carboxyl group by an uncharged amide, as in the glutamine mutant, were shown to virtually abolish activity. This implied that the precise spatial position and charge of the carboxyl group are crucial for catalysis.

J Bioi Chem 258: 14647-14651 Siegall CB, Chaudhary VK, FitzGerald DJ, Past an I (1989) Functional analysis of domains II, Ib, and III of Pseudomonas exotoxin. J Bioi Chem 264: 14256-14261 Sigler PB, Druyan ME, Kiefer HC, Finkelstein RA (1977) Cholera toxin crystals suitable for X-ray diffraction. Science 197: 1277-1279 Simpson LI (1989) The binary toxin produced by Clostridium botulinum enters cells by receptor-mediated endocytosis to exert its pharmacologic effects. J Pharmacol Exp Ther 251: 1223-1228 Sixma TK, Pronk SE, Kalk KH, Wartna ES, Van Zanten BAM, Witholt B, Hoi WGJ (1991) Crystal structure of cholera toxin related heat labile enterotoxin from E.

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


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