Metacaspase

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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, paracaspases and orthocaspases can be considered sub-classes among the metacaspases. Common for all three classes are 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.

Type I[edit]

Type I metacaspases are characterized by an amino-terminal proline or glutamine rich LSD zinc finger-like domain.[4] This class can almost exclusively be found in plants, with one recent exception where both type I and type II metacaspases were found in the genome of Monosiga brevicollis (Choanoflagellate),[5] possibly as a result of an unusual horizontal gene transfer between two eukaryotes.

Type II[edit]

Type II has a wider phylogenetic distribution among all eukaryotes except those where paracaspases have been found (animals and slime mold). This group is characterized by lacking an amino-terminal domain.

Known functions[edit]

In an analogous manner to caspases, metacaspases induce programmed cell death in both plants and fungi (yeast).[6][7][8]

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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. doi:10.1371/journal.pone.0049888. PMC 3501461Freely accessible. PMID 23185476. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. doi:10.1073/pnas.0506948102. PMC 1242326Freely accessible. PMID 16183741. 
  8. ^ 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. doi:10.1073/pnas.0508120102. PMC 1287485Freely accessible. PMID 16301538. 

See also[edit]