JXB Advance Access published online on February 13, 2008
Journal of Experimental Botany, doi:10.1093/jxb/erm352
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FOCUS REVIEW PAPER |
What happened to plant caspases?
1Faculty of Life Sciences, University of Manchester, 3.614 Stopford Building, Oxford Road, Manchester M13 9PT, UK
2UMR Plante-Microbe-Environnement, INRA 1088/CNRS 5184/U-Bourgogne, BP 86510, 21065 Dijon Cedex, France
* To whom correspondence should be addressed. E-mail: patrick.gallois{at}manchester.ac.uk
The extent of conservation in the programmed cell death pathways that are activated in species belonging to different kingdoms is not clear. Caspases are key components of animal apoptosis; caspase activities are detected in both animal and plant cells. Yet, while animals have caspase genes, plants do not have orthologous sequences in their genomes. It is 10 years since the first caspase activity was reported in plants, and there are now at least eight caspase activities that have been measured in plant extracts using caspase substrates. Various caspase inhibitors can block many forms of plant programmed cell death, suggesting that caspase-like activities are required for completion of the process. Since plant metacaspases do not have caspase activities, a major challenge is to identify the plant proteases that are responsible for the caspase-like activities and to understand how they relate, if at all, to animal caspases. The protease vacuolar processing enzyme, a legumain, is responsible for the cleavage of caspase-1 synthetic substrate in plant extracts. Saspase, a serine protease, cleaves caspase-8 and some caspase-6 synthetic substrates. Possible scenarios that could explain why plants have caspase activities without caspases are discussed.
Key words: Caspase-like, metacaspases, plants, programmed cell death, protease
Received 20 November 2007; Revised 11 December 2007 Accepted 13 December 2007
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