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Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine

(2004) JOURNAL OF BIOLOGICAL CHEMISTRY. 279(44). p.45329-45336
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Abstract
Nine potential caspase counterparts, designated metacaspases, were identified in the Arabidopsis thaliana genome. Sequence analysis revealed two types of metacaspases, one with ( type I) and one without ( type II) a proline- or glutamine-rich N-terminal extension, possibly representing a prodomain. Production of recombinant Arabidopsis type II metacaspases in Escherichia coli resulted in cysteine-dependent autocatalytic processing of the proform into large and small subunits, in analogy to animal caspases. A detailed biochemical characterization with a broad range of synthetic oligopeptides and several protease inhibitors of purified recombinant proteins of both metacaspase 4 and 9 showed that both metacaspases are arginine/lysine-specific cysteine proteases and did not cleave caspase-specific synthetic substrates. These findings suggest that type II metacaspases are not directly responsible for earlier reported caspase-like activities in plants.
Keywords
PROTEASES, ACTIVATION, APOPTOSIS, INVOLVEMENT, PLANT-CELLS, TOBACCO CELLS, CRYSTAL-STRUCTURE, TRACHEARY ELEMENTS, PROGRAMMED CELL-DEATH, CASPASE-LIKE ACTIVITY

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MLA
Vercammen, Dominique, et al. “Type II Metacaspases Atmc4 and Atmc9 of Arabidopsis Thaliana Cleave Substrates after Arginine and Lysine.” JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 279, no. 44, 2004, pp. 45329–36, doi:10.1074/jbc.M406329200.
APA
Vercammen, D., Van De Cotte, B., De Jaeger, G., Eeckhout, D., Casteels, P., Vandepoele, K., … Van Breusegem, F. (2004). Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine. JOURNAL OF BIOLOGICAL CHEMISTRY, 279(44), 45329–45336. https://doi.org/10.1074/jbc.M406329200
Chicago author-date
Vercammen, Dominique, Brigitte Van De Cotte, Geert De Jaeger, Dominique Eeckhout, Peter Casteels, Klaas Vandepoele, Isabel Vandenberghe, Jozef Van Beeumen, Dirk Inzé, and Frank Van Breusegem. 2004. “Type II Metacaspases Atmc4 and Atmc9 of Arabidopsis Thaliana Cleave Substrates after Arginine and Lysine.” JOURNAL OF BIOLOGICAL CHEMISTRY 279 (44): 45329–36. https://doi.org/10.1074/jbc.M406329200.
Chicago author-date (all authors)
Vercammen, Dominique, Brigitte Van De Cotte, Geert De Jaeger, Dominique Eeckhout, Peter Casteels, Klaas Vandepoele, Isabel Vandenberghe, Jozef Van Beeumen, Dirk Inzé, and Frank Van Breusegem. 2004. “Type II Metacaspases Atmc4 and Atmc9 of Arabidopsis Thaliana Cleave Substrates after Arginine and Lysine.” JOURNAL OF BIOLOGICAL CHEMISTRY 279 (44): 45329–45336. doi:10.1074/jbc.M406329200.
Vancouver
1.
Vercammen D, Van De Cotte B, De Jaeger G, Eeckhout D, Casteels P, Vandepoele K, et al. Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine. JOURNAL OF BIOLOGICAL CHEMISTRY. 2004;279(44):45329–36.
IEEE
[1]
D. Vercammen et al., “Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine,” JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 279, no. 44, pp. 45329–45336, 2004.
@article{298618,
  abstract     = {{Nine potential caspase counterparts, designated metacaspases, were identified in the Arabidopsis thaliana genome. Sequence analysis revealed two types of metacaspases, one with ( type I) and one without ( type II) a proline- or glutamine-rich N-terminal extension, possibly representing a prodomain. Production of recombinant Arabidopsis type II metacaspases in Escherichia coli resulted in cysteine-dependent autocatalytic processing of the proform into large and small subunits, in analogy to animal caspases. A detailed biochemical characterization with a broad range of synthetic oligopeptides and several protease inhibitors of purified recombinant proteins of both metacaspase 4 and 9 showed that both metacaspases are arginine/lysine-specific cysteine proteases and did not cleave caspase-specific synthetic substrates. These findings suggest that type II metacaspases are not directly responsible for earlier reported caspase-like activities in plants.}},
  author       = {{Vercammen, Dominique and Van De Cotte, Brigitte and De Jaeger, Geert and Eeckhout, Dominique and Casteels, Peter and Vandepoele, Klaas and Vandenberghe, Isabel and Van Beeumen, Jozef and Inzé, Dirk and Van Breusegem, Frank}},
  issn         = {{0021-9258}},
  journal      = {{JOURNAL OF BIOLOGICAL CHEMISTRY}},
  keywords     = {{PROTEASES,ACTIVATION,APOPTOSIS,INVOLVEMENT,PLANT-CELLS,TOBACCO CELLS,CRYSTAL-STRUCTURE,TRACHEARY ELEMENTS,PROGRAMMED CELL-DEATH,CASPASE-LIKE ACTIVITY}},
  language     = {{eng}},
  number       = {{44}},
  pages        = {{45329--45336}},
  title        = {{Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine}},
  url          = {{http://dx.doi.org/10.1074/jbc.M406329200}},
  volume       = {{279}},
  year         = {{2004}},
}

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