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Death by proteases in plants: whodunit
Author(s) -
Rotari Vitalie I.,
He Rui,
Gallois Patrick
Publication year - 2005
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.2005.00465.x
Subject(s) - proteases , caspase , protease , programmed cell death , biology , dna laddering , vacuole , microbiology and biotechnology , apoptosis , nlrp1 , cytoplasm , biochemistry , enzyme , dna fragmentation
Several studies have shown that protease inhibitors can suppress programmed cell death in various plant species and plant tissues. This is especially true of caspase inhibitors that can block programmed cell death and its marker DNA laddering. There are up to six different caspase‐like activities that can be measured in plant extracts, the most prominent being caspase1‐like and caspase3‐like. These activities can be located in vacuoles and also in the nucleus or the cytoplasm. This represents a striking apparent similarity with animal programmed cell death. Because there are no caspase orthologue in plant genomes, a major challenge is to identify these proteases. Recently two proteases with caspase‐like activities have been recognized as belonging to two different protease families that are not closely related to animal caspases. Various other protease families have been implicated and this suggests that complex protease networks have been recruited for the plant cell demise.