Metacaspase
From Wikipedia the free encyclopedia
Metacaspases are members of the C14 class of cysteine proteases and thus related to caspases, orthocaspases and paracaspases.[1] The metacaspases are arginine/lysine-specific, in contrast to caspases, which are aspartate-specific.[2]
Structure and Phylogenetic distribution[edit]
Prokaryotes[edit]
In archea and bacteria, there are several metacaspases with a wide range of domain organizations.[3] Based on the prokaryote metacaspase diversity, orthocaspases can be considered a sub-class of metacaspases. Common for both metacaspases and orthocaspases classes is their specificity for basic residues (arginine or lysine) in the P1 position. At this moment, no structural variants have been reported where the substrate specificity would change to an acidic residue (aspartic acid), like in true caspases.
Eukaryotes[edit]
Metacaspases are found in plants, fungi, and "protists", but not in slime mold or animals.
Viruses[edit]
Viral metacaspases, which may have implications in rewiring host metabolism to enhance infection, are widespread in the ocean.[4]
Type I[edit]
Type I metacaspases are characterized by an amino-terminal proline or glutamine rich LSD zinc finger-like domain.[5] This type can be found in prokaryotes and eukaryotes other than animals.
Type II[edit]
Type II is found only in certain green algae and land plants, with one recent exception where both type I and type II metacaspases were found in the genome of Monosiga brevicollis (Choanoflagellate),[6] possibly as a result of an unusual horizontal gene transfer between two eukaryotes.This group is characterized by long linker region and the absence of an amino-terminal pro-domain.
Known functions[edit]
In an analogous manner to caspases, metacaspases induce programmed cell death in both plants and fungi (yeast).[7][8][9]
References[edit]
- ^ Uren AG, O'Rourke K, Aravind LA, et al. (Oct 2000). "Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma". Molecular Cell. 6 (4): 961–7. doi:10.1016/S1097-2765(05)00086-9. PMID 11090634.
- ^ Vercammen D, van de Cotte B, De Jaeger G, et al. (Oct 2004). "Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine". J Biol Chem. 279 (44): 45329–36. doi:10.1074/jbc.M406329200. PMID 15326173.
- ^ Asplund-Samuelsson J, Bergman B, Larsson J (Nov 2012). "Prokaryotic caspase homologs: phylogenetic patterns and functional characteristics reveal considerable diversity". PLOS ONE. 7 (11): e49888. Bibcode:2012PLoSO...749888A. doi:10.1371/journal.pone.0049888. PMC 3501461. PMID 23185476.
- ^ Wilson W, et al. (2017). "Genomic exploration of individual giant ocean viruses". The ISME Journal. 11 (8): 1736–1745. doi:10.1038/ismej.2017.61. PMC 5520044. PMID 28498373.
- ^ Vercammen D, van de Cotte B, De Jaeger G, et al. (Oct 2004). "Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine". J Biol Chem. 279 (44): 45329–36. doi:10.1074/jbc.M406329200. PMID 15326173.
- ^ Nedelcu AM, Miles IH, Fagir AM, Karol K (Aug 2008). "Adaptive eukaryote-to-eukaryote lateral gene transfer: stress-related genes of algal origin in the closest unicellular relatives of animals". J Evol Biol. 21 (6): 1852–60. doi:10.1111/j.1420-9101.2008.01605.x. PMID 18717747.
- ^ Madeo F, Herker E, Maldener C, et al. (Apr 2002). "A caspase-related protease regulates apoptosis in yeast". Molecular Cell. 9 (4): 911–7. doi:10.1016/S1097-2765(02)00501-4. PMID 11983181.
- ^ Bozhkov PV, Suarez MF, Filonova LH, et al. (Oct 2005). "Cysteine protease mcII-Pa executes programmed cell death during plant embryogenesis". Proc Natl Acad Sci U S A. 102 (40): 14463–8. Bibcode:2005PNAS..10214463B. doi:10.1073/pnas.0506948102. PMC 1242326. PMID 16183741.
- ^ Khan MA, Chock PB, Stadtman ER (Nov 2005). "Knockout of caspase-like gene, YCA1, abrogates apoptosis and elevates oxidized proteins in Saccharomyces cerevisiae". Proc Natl Acad Sci U S A. 102 (48): 17326–31. Bibcode:2005PNAS..10217326K. doi:10.1073/pnas.0508120102. PMC 1287485. PMID 16301538.