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Review
. 2005 Mar;137(3):841-7.
doi: 10.1104/pp.104.058552.

Caspases. Regulating death since the origin of life

Maite Sanmartín  1 , Lukasz Jaroszewski, Natasha V Raikhel, Enrique Rojo
Affiliations
Review

Caspases. Regulating death since the origin of life

Maite Sanmartín et al. Plant Physiol. 2005 Mar.
No abstract available

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Figures

Figure 1.
Figure 1.
The model VPEγ based on human caspase-8. A, The sequence of VPEγ was submitted to FFAS03 (Jaroszewski et al., 2000) and SUPERFAMILY (Gough et al., 2001) fold prediction servers. Both FFAS03 and SUPERFAMILY listed caspase fold as the most probable fold for the central region of VPEγ sequence (residues 50–330), and selected caspase-8 as the structure most similar to VPEγ. The alignment from FFAS03 was used for modeling using caspase-8 as a structural template. The model of the VPEγ molecule was built with the MODELER program. Residues aligned with binding site residues of caspase-8 are shown as spheres. B, The active site interactions in human caspase-8 (left) and predicted active site interactions in VPEγ (right). Replacement of Gln residue with Glu residue is connected with difference in specificity between caspases and VPEs (Asp and Asn residues in P1 position of the substrate, respectively).
Figure 2.
Figure 2.
Domain structure of plant VPEs and metacaspases. The position of the His-Cys catalytic dyad of these enzymes is shown. VPEs are synthesized as inactive zymogens with a signal peptide for insertion into the endomembrane system. The inhibitory C-terminal propeptide and the N-terminal propeptide of VPEs are sequentially removed, most likely in the acidic environment of the vacuole. Metacaspases are probably cytosolic enzymes that may be autoprocessed into 2 subunits, p20 and p10. In addition, type I metacaspases contain a prodomain rich in Pro and Gln residues, which contain a zinc finger motif similar to the ones present in LSD1, a negative regulator of PCD in Arabidopsis.
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References

    1. Aravind L, Koonin E (2002) Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins. Proteins 46: 355–367 - PubMed
    1. Bozhkov PV, Filonova LH, Suarez MF, Helmersson A, Smertenko AP, Zhivotovsky B, von Arnold S (2004) VEIDase is a principal caspase-like activity involved in plant programmed cell death and essential for embryonic pattern formation. Cell Death Differ 11: 175–182 - PubMed
    1. Coffeen WC, Wolpert TJ (2004) Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa. Plant Cell 16: 857–873 - PMC - PubMed
    1. Danon A, Rotari VI, Gordon A, Mailhac N, Gallois P (2004) 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. J Biol Chem 279: 779–787 - PubMed
    1. Dickman MB, Park YK, Oltersdorf T, Li W, Clemente T, French R (2001) Abrogation of disease development in plants expressing animal antiapoptotic genes. Proc Natl Acad Sci USA 98: 6957–6962 - PMC - PubMed

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