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Bioscience, Biotechnology, and Biochemistry Volume 63, 1999 - Issue 9
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Original Articles

Contribution of Histidine Residues to Oligomerization of θ-Toxin (Perfringolysin O), a Cholesterol-Binding Cytolysin

Megumi NAKAMURAProtein Biochemistry, Tokyo Metropolitan Institute of Gerontology
,
Naoko SEKINO-SUZUKIProtein Biochemistry, Tokyo Metropolitan Institute of Gerontology
,
Yukiko SHIMADAProtein Biochemistry, Tokyo Metropolitan Institute of Gerontology
&
Yoshiko OHNO-IWASHITAProtein Biochemistry, Tokyo Metropolitan Institute of Gerontology
Pages 1640-1643 | Received 23 Mar 1999, Accepted 13 May 1999, Published online: 22 May 2014

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  • 2) Rossjohn, J., Feil, S. C., Mckinstry, W. J., Tweten, R. K., and Parker, M. W., Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell, 89, 685-692 (1997).
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  • 9) Ohno-Iwashita, Y., Iwamoto, M., Ando, S., Mitsui, K., and Iwashita, S., A modified theta-toxin produced by limited proteolysis and methylation: a probe for the functional study of membrane cholesterol. Biochim. Biophys. Acta, 1023, 441-448 (1990).
  • 10) Ohno-Iwashita, Y., Iwamoto, M., Mitsui, K., Kawasaki, H., and Ando, S., Cold-labile hemolysin produced by limited proteolysis of θ-toxin from Clostridium perfringens. Biochemistry, 25, 6048-6053 (1986).
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