Journal Article

What happened to plant caspases?

Laurent Bonneau, Yuan Ge, Georgina E. Drury and Patrick Gallois

in Journal of Experimental Botany

Published on behalf of Society for Experimental Biology

Volume 59, issue 3, pages 491-499
Published in print February 2008 | ISSN: 0022-0957
Published online February 2008 | e-ISSN: 1460-2431 | DOI: https://dx.doi.org/10.1093/jxb/erm352
What happened to plant caspases?

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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.

Keywords: Caspase-like; metacaspases; plants; programmed cell death; protease

Journal Article.  5398 words. 

Subjects: Plant Sciences and Forestry

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