Metacaspase

Last updated November 29, 2024

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. ^{[ citation needed ]}

Eukaryotes

Metacaspases are found in plants, fungi, and "protists", but not in slime mold or animals. ^{[ citation needed ]}

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. ^{[ citation needed ]}

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. ^{[ citation needed ]}

Known functions

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

Related Research Articles

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Eukaryotic translation initiation factor 4 gamma 2 is a protein that in humans is encoded by the EIF4G2 gene.

Kexin is a prohormone-processing protease, specifically a yeast serine peptidase, found in the budding yeast. It catalyzes the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process yeast alpha-factor pheromone and killer toxin precursors. The human homolog is PCSK4. It is a family of subtilisin-like peptidases. Even though there are a few prokaryote kexin-like peptidases, all kexins are eukaryotes. The enzyme is encoded by the yeast gene KEX2, and usually referred to in the scientific community as Kex2p. It shares structural similarities with the bacterial protease subtilisin. The first mammalian homologue of this protein to be identified was furin. In the mammal, kexin-like peptidases function in creating and regulating many differing proproteins.

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<span class="mw-page-title-main">Protein arginine methyltransferase 5</span> Protein-coding gene in the species Homo sapiens

Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene. PRMT5 symmetrically dimethylates H2AR3, H4R3, H3R2, and H3R8 in vivo, all of which are linked to a range of transcriptional regulatory events.

NLRP1 encodes NACHT, LRR, FIIND, CARD domain and PYD domains-containing protein 1 in humans. NLRP1 was the first protein shown to form an inflammasome. NLRP1 is expressed by a variety of cell types, which are predominantly epithelial or hematopoietic. The expression is also seen within glandular epithelial structures including the lining of the small intestine, stomach, airway epithelia and in hairless or glabrous skin. NLRP1 polymorphisms are associated with skin extra-intestinal manifestations in CD. Its highest expression was detected in human skin, in psoriasis and in vitiligo. Polymorphisms of NLRP1 were found in lupus erythematosus and diabetes type 1. Variants of mouse NLRP1 were found to be activated upon N-terminal cleavage by the protease in anthrax lethal factor.

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Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene.

Sentrin-specific protease 2 is an enzyme that in humans is encoded by the SENP2 gene.

Mucosa-associated lymphoid tissue lymphoma translocation protein 1 is a protein that in humans is encoded by the MALT1 gene. It's the human paracaspase.

Histone acetyltransferase 1, also known as HAT1, is an enzyme that, in humans, is encoded by the HAT1 gene.

Signal peptidase I is an enzyme. This enzyme catalyses the following chemical reaction

Rhomboid-related protein 2 is a protein that in humans is encoded by the RHBDL2 gene.

References

↑ 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.