Trends in Plant Science
UpdateResearch FocusDeath proteases: alive and kicking
Section snippets
Structural similarities between PCD in animal and plant cells
Programmed cell death (PCD) in animal cells is often executed by caspases. Caspases belong to a class of specific cysteine proteases that show a high degree of specificity, with an absolute requirement for cleavage adjacent to an aspartate residue and a recognition sequence comprised of at least four amino acids N-terminal to this cleavage site. In animal cells, a number of morphological and biochemical features accompanying cell death (e.g. chromatin condensation and nuclear and DNA
The plant proteasome confers caspase-like activity
The 26S proteasome is responsible for the breakdown of the majority of proteins and consists of the 20S proteasome and one or two 19S regulatory complexes. The 20S proteasome is a hollow cylinder composed of four stacked rings; the two inner beta rings are identical in subunit composition and each beta ring contains three different proteolytic sites designated β1, β2 and β5. Previously it was shown that animal and yeast (Saccharomyces cerevisiae) proteasomes show caspase-like activity. These
Type II metacaspase cleaves a conserved caspase3 substrate
Metacaspases (MCAs) are cysteine proteases that show structural similarity to caspases (specifically the caspase hemoglobinase fold) but instead of cleavage adjacent to Asp, MCAs show a proteolytic activity against arginine and lysine in the P1 position. Arabidopsis has nine MCA genes; three of type I and six of type II. Type I MCAs have an N-terminal extension reminiscent of the prodomain of initiator caspases. This prodomain contains two putative CXXC-type zinc finger structures similar to
Death protease diversity and substrate conservation?
The cell death machinery in plants seems more divergent than in animal cells, where cell death is often executed through the coordinated action of a small family of structurally related cysteine proteases (caspases). Plant cells apparently employ a wide range of structurally unrelated proteases that, surprisingly, show a caspase-like preference for specific (conserved) sequences in their substrates. Currently a number of death proteases have been identified. For most of these proteases the cell
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Cited by (41)
Plant defence mechanisms against mycotoxin Fumonisin B1
2021, Chemico-Biological InteractionsCitation Excerpt :It is known that FB1-induced ROS accumulation was highly dependent on the presence of light suggesting the key role of chloroplast in defence responses [44,80]. ROS play an elementary role in the initiation of plant PCD which is mediated by various nucleases and proteases [97,114,115]. It was found that the metacaspase-coding sequences such as AtMC3, AtMC8, and AtMC9 were also expressed within 24 h upon 10 μM FB1 infiltration [121].
Cell death signaling and morphology in chemical-treated tobacco BY-2 suspension cultured cells
2019, Environmental and Experimental BotanyCitation Excerpt :Mixed features of apoptotic-like and vacuolar cell deaths are observed, for example, in the hypersensitive response (HR) occurring as a rapid local cell death at the primary site of microbial attack (Levine et al., 1994; Heath, 2000; Mur et al., 2008; van Doorn and Woltering, 2010). Plant PCD may or may not involve caspase-like proteolytic enzymes (CLPs) which are functional homologues to cysteine-aspartic proteases (caspases) playing a critical role in cell death in animal systems through the activation of specific DNAses responsible for DNA cleavage into oligonucleosomal units of 180 bp and multiples thereof (laddering pattern) (Lockshin et al., 2000; van Doorn and Woltering, 2004; Bonneau et al., 2008; Woltering, 2010). Collectively, the knowledge on plant PCD points out that depending on the plant system, the nature and severity of inducing factors (internal and/or external), the cell death may engage similar, distinct or overlapping signal transduction cascades leading to specific or mixed morphological occurrence.
Aluminium-induced cell death requires upregulation of NtVPE1 gene coding vacuolar processing enzyme in tobacco (Nicotiana tabacum L.)
2018, Journal of Inorganic BiochemistryFlower Senescence
2016, Encyclopedia of Applied Plant SciencesDihydrotanshinone i induced apoptosis and autophagy through caspase dependent pathway in colon cancer
2015, PhytomedicineCitation Excerpt :Caspases can be divided into two distinct groups, the initiator caspases including caspase-8 and -9 as well as the executioner caspases, such as caspase-3 and -7. Initiator caspases are present in the cell as inactive monomers and their activation is promoted by dimerization, which happens when initiator caspases are recruited to large molecular weight protein complexes that act as signaling platforms (Fan et al., 2005; Lamkanfi and Kanneganti, 2010; Tait and Green, 2010; Woltering, 2010). Caspase-2 has been reported as an initiator caspase, its role is very special in apoptosis since caspase-2 gene produces several alternative splicing isoforms (Bouchier-Hayes and Green, 2012).