|
Originally published In Press as doi:10.1074/jbc.M504476200 on July 25, 2005
J. Biol. Chem., Vol. 280, Issue 38, 32914-32920, September 23, 2005
Vacuolar Processing Enzyme Is Essential for Mycotoxin-induced Cell Death in Arabidopsis thaliana*
Miwa Kuroyanagi ,
Kenji Yamada ,
Noriyuki Hatsugai ,
Maki Kondo ,
Mikio Nishimura , and
Ikuko Hara-Nishimura 1
From the
Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan and Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan
Some compatible pathogens secrete toxins to induce host cell death and promote their growth. The toxin-induced cell death is a pathogen strategy for infection. To clarify the executioner of the toxin-induced cell death, we examined a fungal toxin (fumonisin B1 (FB1))-induced cell death of Arabidopsis plants. FB1-induced cell death was accompanied with disruption of vacuolar membrane followed by lesion formation. The features of FB1-induced cell death were completely abolished in the Arabidopsis vacuolar processing enzyme (VPE)-null mutant, which lacks all four VPE genes of the genome. Interestingly, an inhibitor of caspase-1 abolished FB1-induced lesion formation, as did a VPE inhibitor. The VPE-null mutant had no detectable activities of caspase-1 or VPE in the FB1-treated leaves, although wild-type leaves had the caspase-1 and VPE activities, both of which were inhibited by a caspase-1 inhibitor. VPE is the most essential among the four VPE homologues for FB1-induced cell death in Arabidopsis leaves. Recombinant VPE recognized a VPE substrate with Km = 30.3 µM and a caspase-1 substrate with Km = 44.2 µM, which is comparable with the values for mammalian caspase-1. The VPE precursor was self-catalytically converted into the mature form exhibiting caspase-1 activity. These in vivo and in vitro analyses demonstrate that VPE is the proteinase that exhibits a caspase-1 activity. We show that VPE exhibiting a caspase-1 activity is a key molecule in toxin-induced cell death. Our findings suggest that a susceptible response of toxin-induced cell death is caused by the VPE-mediated vacuolar mechanism similar to a resistance response of hypersensitive cell death (Hatsugai, N., Kuroyanagi, M., Yamada, K., Meshi, T., Tsuda, S., Kondo, M., Nishimura, M., and Hara-Nishimura, I. (2004) Science 305, 855858).
Received for publication, April 25, 2005
, and in revised form, July 25, 2005.
* This work was supported by Core Research for Evolutional Science and Technology of the Japan Science and Technology Corporation, Grants-in-aid for Scientific Research 16085203 and 16657013 and 17107002, 21st Century Center of Excellence Research Kyoto University (A14) from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and Postdoctoral Fellowship 15008768 from the Japan Society for the Promotion of Science (to M. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbs.org) contains supplemental Figs. 1 and 2.
1 To whom correspondence should be addressed. Tel.: 81-75-753-4142; Fax: 81-75-753-4142; E-mail: ihnishi{at}gr.bot.kyoto-u.ac.jp.

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
H. P. van Esse, J. W. van't Klooster, M. D. Bolton, K. A. Yadeta, P. van Baarlen, S. Boeren, J. Vervoort, P. J.G.M. de Wit, and B. P.H.J. Thomma
The Cladosporium fulvum Virulence Protein Avr2 Inhibits Host Proteases Required for Basal Defense
PLANT CELL,
July 1, 2008;
20(7):
1948 - 1963.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
J. Li, G. Brader, and E. T. Palva
Kunitz Trypsin Inhibitor: An Antagonist of Cell Death Triggered by Phytopathogens and Fumonisin B1 in Arabidopsis
Mol Plant,
May 1, 2008;
1(3):
482 - 495.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
A. Kuthanova, Z. Opatrny, and L. Fischer
Is internucleosomal DNA fragmentation an indicator of programmed death in plant cells?
J. Exp. Bot.,
May 1, 2008;
59(8):
2233 - 2240.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
L. Bonneau, Y. Ge, G. E. Drury, and P. Gallois
What happened to plant caspases?
J. Exp. Bot.,
February 13, 2008;
(2008)
erm352v1.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
I. Saska, A. D. Gillon, N. Hatsugai, R. G. Dietzgen, I. Hara-Nishimura, M. A. Anderson, and D. J. Craik
An Asparaginyl Endopeptidase Mediates in Vivo Protein Backbone Cyclization
J. Biol. Chem.,
October 5, 2007;
282(40):
29721 - 29728.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. Quattrocchio, W. Verweij, A. Kroon, C. Spelt, J. Mol, and R. Koes
PH4 of Petunia Is an R2R3 MYB Protein That Activates Vacuolar Acidification through Interactions with Basic-Helix-Loop-Helix Transcription Factors of the Anthocyanin Pathway
PLANT CELL,
May 1, 2006;
18(5):
1274 - 1291.
[Abstract]
[Full Text]
[PDF]
|
 |
|
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|