Ultraviolet-C overexposure induces programmed cell death in Arabidopsis, which is mediated by caspase-like activities and which can be suppressed by caspase inhibitors, p35 and Defender against Apoptotic Death.
Plants, animals, and several branches of unicellular eukaryotes use programmed cell death (PCD) for defense or developmental mechanisms. This argues for a common ancestral apoptotic system in eukaryotes. However, at the molecular level, very few regulatory proteins or protein domains have been identified as conserved across all eukaryotic PCD forms. A very important goal is to determine which molecular components may be used in the execution of PCD in plants, which have been conserved during evolution, and which are plant-specific. Using Arabidopsis thaliana, we have shown that UV radiation can induce apoptosis-like changes at the cellular level and that a UV experimental system is relevant to the study of PCD in plants. We report here that UV induction of PCD required light and that a protease cleaving the caspase substrate Asp-Glu-Val-Asp (DEVDase activity) was induced within 30 min and peaked at 1 h. This DEVDase appears to be related to animal caspases at the biochemical level, being insensitive to broad-range cysteine protease inhibitors. In addition, caspase-1 and caspase-3 inhibitors and the pan-caspase inhibitor p35 were able to suppress DNA fragmentation and cell death. These results suggest that a YVADase activity and an inducible DEVDase activity possibly mediate DNA fragmentation during plant PCD induced by UV overexposure. We also report that At-DAD1 and At-DAD2, the two A. thaliana homologs of Defender against Apoptotic Death-1, could suppress the onset of DNA fragmentation in A. thaliana, supporting an involvement of the endoplasmic reticulum in this form of the plant PCD pathway.
Danon
Antoine
A
Laboratoire Génome et Développement des Plantes, CNRS, Unité Mixte de Recherche 5096, Université de Perpignan, 52 Avenue de Villeneuve, 66860 Perpignan Cedex, France.
Rotari
Vitalie I
VI
Gordon
Anna
A
Mailhac
Nathalie
N
Gallois
Patrick
P
D000595:Amino Acid Sequence; D017209:Apoptosis / Q000528:radiation effects*; D051017:Apoptosis Regulatory Proteins; D017360:Arabidopsis / Q000235:genetics / Q000502:physiology / Q000528:radiation effects*; D001483:Base Sequence; D029742:Caenorhabditis elegans Proteins; D061945:Caspase Inhibitors; D020169:Caspases / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D017931:DNA Primers; D018744:DNA, Plant / Q000737:chemistry / Q000528:radiation effects; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology; D030821:Plants, Genetically Modified / Q000235:genetics / Q000528:radiation effects; D016133:Polymerase Chain Reaction; D011523:Protoplasts / Q000528:radiation effects; D012097:Repressor Proteins / Q000235:genetics / Q000502:physiology*; D014162:Transfection; D014466:Ultraviolet Rays
D051017:Apoptosis Regulatory Proteins; D029742:Caenorhabditis elegans Proteins; D061945:Caspase Inhibitors; D015853:Cysteine Proteinase Inhibitors; D017931:DNA Primers; D018744:DNA, Plant; C096021:Dad-1 protein, C elegans; D009842:Oligopeptides; D012097:Repressor Proteins; C108637:aspartyl-glutamyl-valyl-aspartal; C118632:tyrosyl-valyl-alanyl-aspartal; D020169:Caspases