Biology:Metacaspase

From HandWiki

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

Prokaryotes

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

Metacaspases are found in plants, fungi, and "protists", but not in slime mold or animals.

Viruses

Viral metacaspases, which may have implications in rewiring host metabolism to enhance infection, are widespread in the ocean.[4]

Type I

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

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

In an analogous manner to caspases, metacaspases induce programmed cell death in both plants and fungi (yeast).[7][8][9]

References

  1. ↑ "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. Oct 2000. doi:10.1016/S1097-2765(05)00086-9. PMID 11090634. 
  2. ↑ "Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine". J Biol Chem 279 (44): 45329–36. Oct 2004. doi:10.1074/jbc.M406329200. PMID 15326173. 
  3. ↑ "Prokaryotic caspase homologs: phylogenetic patterns and functional characteristics reveal considerable diversity.". PLOS ONE 7 (11): e49888. Nov 2012. doi:10.1371/journal.pone.0049888. PMID 23185476. Bibcode: 2012PLoSO...749888A. 
  4. ↑ "Genomic exploration of individual giant ocean viruses.". The ISME Journal 11 (8): 1736–1745. 2017. doi:10.1038/ismej.2017.61. PMID 28498373. 
  5. ↑ "Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine". J Biol Chem 279 (44): 45329–36. Oct 2004. doi:10.1074/jbc.M406329200. PMID 15326173. 
  6. ↑ "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. Aug 2008. doi:10.1111/j.1420-9101.2008.01605.x. PMID 18717747. 
  7. ↑ "A caspase-related protease regulates apoptosis in yeast". Molecular Cell 9 (4): 911–7. Apr 2002. doi:10.1016/S1097-2765(02)00501-4. PMID 11983181. 
  8. ↑ "Cysteine protease mcII-Pa executes programmed cell death during plant embryogenesis". Proc Natl Acad Sci U S A 102 (40): 14463–8. Oct 2005. doi:10.1073/pnas.0506948102. PMID 16183741. Bibcode: 2005PNAS..10214463B. 
  9. ↑ "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. Nov 2005. doi:10.1073/pnas.0508120102. PMID 16301538. Bibcode: 2005PNAS..10217326K. 

See also



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