Characterization of the Enzymatic Component of Clostridium

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ported the purification of iota-toxin from cultures of C. per- fringens type E. ..... purified variant components showed only one band of approx- imately 43 kDa on ...
JOURNAL OF BACTERIOLOGY, Apr. 2000, p. 2096–2103 0021-9193/00/$04.00⫹0 Copyright © 2000, American Society for Microbiology. All Rights Reserved.

Vol. 182, No. 8

Characterization of the Enzymatic Component of Clostridium perfringens Iota-Toxin MASAHIRO NAGAHAMA, YOSHIHIKO SAKAGUCHI, KEIKO KOBAYASHI, SADAYUKI OCHI, AND JUN SAKURAI* Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Tokushima 770-8514, Japan Received 4 October 1999/Accepted 20 January 2000

The iotaa component (ia) of Clostridium perfringens ADP ribosylates nonmuscle ␤/␥ actin and skeletal muscle ␣-actin. Replacement of Arg-295 in ia with alanine led to a complete loss of NADⴙ-glycohydrolase (NADase) and ADP-ribosyltransferase (ARTase); that of the residue with lysine caused a drastic reduction in NADase and ARTase activities (