![]()
|
|
||||||||
J Biol Chem, Vol. 275, Issue 2, 823-827, January 14, 2000
From the Thionins are small cysteine-containing,
amphipathic plant proteins found in seeds and vegetative tissues of a
number of plant genera. Many of them have been shown to be toxic to
microorganisms such as fungi, yeast, and bacteria and also to mammalian
cells. It has been suggested that thionins are present in seeds to
protect them, and the germinating seedling, from attack by
phytopathogenic microorganisms, but the mechanism by which they kill
cells remains unclear. Using electrophysiological measurements, we have
shown that The atomic coordinates and structure factors (code 1BHP) have
been deposited in the Protein Data Bank, Research Collaboratory for
Structural Bioinformatics, Rutgers University, New Brunswick, NJ
(http://www.rcsb.org/).
The Cytotoxic Plant Protein,
-Purothionin, Forms Ion
Channels in Lipid Membranes*
§¶,
,
, and
CSIRO Plant Industry, Clunies Ross St.,
Canberra, Australian Capital Territory 2601, Australia, the
§ Division of Botany and Zoology, Australian National
University, Canberra, Australian Capital Territory 0200, Australia,
and the ** Membrane Biology Program, John Curtin School of Medical
Research, Australian National University P. O. Box 334, Canberra,
Australian Capital Territory 2601, Australia
-purothionin from wheat flour can form cation-selective ion channels in artificial lipid bilayer membranes and in the plasmalemma of rat hippocampal neurons. We suggest that the generalized toxicity of thionins is due to their ability to generate ion channels in cell membranes, resulting in the dissipation of ion concentration gradients essential for the maintenance of cellular homeostasis.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
61-2-62465470; Fax: 61-2-62465000; Danny.Llewellyn@pi.csiro.au.
This article has been cited by other articles:
![]() |
M. Vila-Perello, A. Sanchez-Vallet, F. Garcia-Olmedo, A. Molina, and D. Andreu Structural Dissection of a Highly Knotted Peptide Reveals Minimal Motif with Antimicrobial Activity J. Biol. Chem., January 14, 2005; 280(2): 1661 - 1668. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. Giudici, R. Pascual, L. de la Canal, K. Pfuller, U. Pfuller, and J. Villalain Interaction of Viscotoxins A3 and B with Membrane Model Systems: Implications to Their Mechanism of Action Biophys. J., August 1, 2003; 85(2): 971 - 981. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Charnet, G. Molle, D. Marion, M. Rousset, and V. Lullien-Pellerin Puroindolines Form Ion Channels in Biological Membranes Biophys. J., April 1, 2003; 84(4): 2416 - 2426. [Abstract] [Full Text] [PDF] |
||||
![]() |
J.-A. Richard, I. Kelly, D. Marion, M. Pezolet, and M. Auger Interaction between beta -Purothionin and Dimyristoylphosphatidylglycerol: A 31P-NMR and Infrared Spectroscopic Study Biophys. J., October 1, 2002; 83(4): 2074 - 2083. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |