title: A plant alternative to animal caspases: subtilisin-like proteases.
abstract: Activities displaying caspase cleavage specificity have been well documented in various plant programmed cell death (PCD) models. However, plant genome analyses have not revealed clear orthologues of caspase genes, indicating that enzyme(s) structurally unrelated yet possessing caspase specificity have functions in plant PCD. Here, we review recent data showing that some caspase-like activities are attributable to the plant subtilisin-like proteases, saspases and phytaspases. These proteases hydrolyze a range of tetrapeptide caspase substrates following the aspartate residue. Data obtained with saspases implicate them in the proteolytic degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) during biotic and abiotic PCD, whereas phytaspase overproducing and silenced transgenics provide evidence that phytaspase regulates PCD during both abiotic (oxidative and osmotic stresses) and biotic (virus infection) insults. Like caspases, phytaspases and saspases are synthesized as proenzymes, which are autocatalytically processed to generate a mature enzyme. However, unlike caspases, phytaspases and saspases appear to be constitutively processed and secreted from healthy plant cells into the intercellular space. Apoplastic localization presumably prevents enzyme-mediated protein fragmentation in the absence of PCD. In response to death-inducing stimuli, phytaspase has been shown to re-localize to the cell interior. Thus, plant PCD-related proteases display both common (D-specific protein fragmentation during PCD) and distinct (enzyme structure and activity regulation) features with animal PCD-related proteases.
authors.affiliation: A N Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russia.
authors.forename: A B
authors.initials: AB
authors.lastname: Vartapetian
authors.forename: A I
authors.initials: AI
authors.lastname: Tuzhikov
authors.forename: N V
authors.initials: NV
authors.lastname: Chichkova
authors.forename: M
authors.initials: M
authors.lastname: Taliansky
authors.forename: T J
authors.initials: TJ
authors.lastname: Wolpert
mesh_terms: D000818:Animals; D017209:Apoptosis / Q000502:physiology; D020169:Caspases / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D010802:Phylogeny; D010940:Plant Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*; D011487:Protein Conformation; D020860:Subtilisin / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*
chemical_list: D015853:Cysteine Proteinase Inhibitors; D007527:Isoenzymes; D010940:Plant Proteins; D020860:Subtilisin; D020169:Caspases