Sheathing the swords of death: Post-translational modulation of plant metacaspases

Zhang, Yi; Lam, Eric

doi:10.4161/psb.6.12.18247

Cited by 22 publications

(17 citation statements)

References 13 publications

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“…The activity of the majority of type I and type II metacaspases characterized to date has been shown to be affected by the presence of calcium ions. Although TbMC2 is the only type I metacaspase requiring high micromolar concentrations of CaCl 2 for activity (Machado et al ., ), yeast type I metacaspase Yca1, as well as type II metacaspases and the type III metacaspases reported here, require millimolar concentrations for full proteolytic activity (Watanabe & Lam, ; Zhang & Lam, ; Piszczek et al ., ). The only exception is the A. thaliana type II metacaspase AtMC9, whose activity has been reported to be calcium independent (Zhang & Lam, ).…”

Section: Discussionmentioning

confidence: 91%

“…Although both type I and type II metacaspases contain the p20 and p10 domains in this order, the newly identified type III metacaspases have an unusual rearrangement of the two domains, resulting in the small p10 domain being located in front of the catalytic p20 domain. Increasing biochemical evidence has shown that the catalytic activity of type I and type II metacaspases depends on the presence of calcium ions, with the only exception of an Arabidopsis thaliana type II metacaspase, AtMC9, whose activity is calcium independent (Zhang & Lam, ). In type II metacaspases, the presence of CaCl 2 in millimolar concentrations induces specific cleavage in the linker region between p20 and p10 domains, similar to the activation observed in caspases (Vercammen et al ., ; Lam & Zhang, ; Piszczek et al ., ).…”

Section: Introductionmentioning

confidence: 99%

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Type III metacaspases: calcium‐dependent activity proposes new function for the p10 domain

Klemenčič

Funk

2017

New Phytologist

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Metacaspases are a subgroup of caspase homologues represented in bacteria, algae and plants. Although type I and type II metacaspases are present in plants, recently discovered and uncharacterized type III metacaspases can only be found in algae which have undergone secondary endosymbiosis. We analysed the expression levels of all 13 caspase homologues in the cryptophyte Guillardia theta in vivo and biochemically characterized its only type III metacaspase, GtMC2, in vitro. Type III metacaspase GtMC2 was shown to be an endopeptidase with a preference for basic amino acids in the P1 position, which exhibited specific N-terminal proteolytic cleavage for full catalytic efficiency. Autolytic processing, as well as the activity of the mature enzyme, required the presence of calcium ions in low millimolar concentrations. In GtMC2, two calcium-binding sites were identified, one with a dissociation constant at low and the other at high micromolar concentrations. We show high functional relatedness of type III metacaspases to type I metacaspases. Moreover, our data suggest that the low-affinity calcium-binding site is located in the p10 domain, which contains a well-conserved N-terminal region. This region can only be found in type I/II/III metacaspases, but is absent in calcium-independent caspase homologues.

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Section: Discussionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Type III metacaspases: calcium‐dependent activity proposes new function for the p10 domain

Klemenčič

Funk

2017

New Phytologist

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“…Studies have also shown that two metacaspases AtMCl and AtMC2 of Arabidopsis play positive and negative regulating roles, respectively, in plant cell death (PCD) (Coll et al, 2010). Although some progress has been made in characterizing the metacaspases (Lam and Zhang, 2012;Tsiatsiani et al, 2011;Vercammen et al, 2007;Zhang and Lam, 2011), a detailed overview of their biochemical properties is still lacking.…”

Section: Introductionmentioning

confidence: 99%

Grapevine VpPR10.1 functions in resistance to Plasmopara viticola through triggering a cell death‐like defence response by interacting with VpVDAC3

Xiang

et al. 2018

Plant Biotechnology Journal

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SummaryAs one of the most serious diseases in grape, downy mildew caused by Plasmopara viticola is a worldwide grape disease. Much effort has been focused on improving susceptible grapevine resistance, and wild resistant grapevine species are important for germplasm improvement of commercial cultivars. Using yeast two‐hybrid screen followed by a series of immunoprecipitation experiments, we identified voltage‐dependent anion channel 3 (VDAC3) protein from Vitis piasezkii ‘Liuba‐8’ as an interacting partner of VpPR10.1 cloned from Vitis pseudoreticulata ‘Baihe‐35‐1’, which is an important germplasm for its resistance to a range of pathogens. Co‐expression of VpPR10.1/VpVDAC3 induced cell death in Nicotiana benthamiana, which accompanied by ROS accumulation. VpPR10.1 transgenic grapevine line showed resistance to P. viticola. We conclude that the VpPR10.1/VpVDAC3 complex is responsible for cell death‐mediated defence response to P. viticola in grapevine.

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“…Although the results from loss‐of‐function analysis with several MC‐encoding genes in yeast and plants are consistent with their role in regulating PCD and stress responses, analogous to the case of caspases in animals, there are also interesting distinctions found between them. One key difference is that all three types of MCs that have been identified and characterized prefer target sites with a basic amino acid residue (arginine or lysine) at the P1 position instead of an aspartate, as in the case for caspases (Vercammen et al ., ; Zhang and Lam, ; Klemencic and Funk, ). Structural studies of type‐I MCs from yeast and protozoa also demonstrated that these enzymes function as monomers instead of dimers in the case of caspases (McLuskey et al ., ; Wong et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Domain swap between two type‐II metacaspases defines key elements for their biochemical properties

Fortin

Lam

2018

The Plant Journal

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Type-II metacaspases are conserved cysteine proteases found in eukaryotes with oxygenic photosynthesis, including green plants and some algae, such as Chlamydomonas and Volvox. Genetic and biochemical studies showed that some members in this protease family could be involved in oxidative stress-induced cell death in higher plants, but their regulatory mechanisms remain unclear. Biochemically, two distinct classes of type-II metacaspases are exemplified by AtMC4 and AtMC9 from Arabidopsis, with AtMC4 activation dependent on calcium under neutral pH, whereas AtMC9 is active only under mildly acidic pH, regardless of the availability of calcium. Here, we constructed all six possible combinations between the p20, linker, and p10 domains from AtMC4 and AtMC9. Our results show that calcium stimulation of AtMC4 activity is associated with essential amino acids located in its p20 domain. In contrast, the acidic pH optimum trait is lost from AtMC9 if one or two of its domains are replaced by that from AtMC4, suggesting that multiple interactions between domains in AtMC9 may be responsible for this property. Consistent with this, we found conserved 'signature' residues in each of the three domains that distinguish AtMC4- and AtMC9-like classes of metacaspases. Tracing the origin of the AtMC9 class, we found evidence for its appearance between lycophytes and gymnosperms, coincident with the evolution of more complex root archetypes in terrestrial plants. Our work suggests that the distinctive properties of the AtMC9-like protease could be associated with special cellular physiology in the roots of gymnosperms and angiosperms that are distinct from lycophytes.

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Sheathing the swords of death: Post-translational modulation of plant metacaspases

Cited by 22 publications

References 13 publications

Type III metacaspases: calcium‐dependent activity proposes new function for the p10 domain

Type III metacaspases: calcium‐dependent activity proposes new function for the p10 domain

Grapevine VpPR10.1 functions in resistance to Plasmopara viticola through triggering a cell death‐like defence response by interacting with VpVDAC3

Domain swap between two type‐II metacaspases defines key elements for their biochemical properties

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