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

Dominique Vercammen UGent, Brigitte Van De Cotte UGent, Geert De Jaeger UGent, Dominique Eeckhout UGent, Peter Casteels UGent, Klaas Vandepoele UGent, Isabel Vandenberghe UGent, Jozef Van Beeumen UGent, Dirk Inzé UGent and Frank Van Breusegem UGent (2004) JOURNAL OF BIOLOGICAL CHEMISTRY. 279(44). p.45329-45336
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
PROTEASES, ACTIVATION, APOPTOSIS, INVOLVEMENT, PLANT-CELLS, TOBACCO CELLS, CRYSTAL-STRUCTURE, TRACHEARY ELEMENTS, PROGRAMMED CELL-DEATH, CASPASE-LIKE ACTIVITY
journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
J. Biol. Chem.
volume
279
issue
44
pages
45329 - 45336
Web of Science type
Article
Web of Science id
000224694900007
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
6.355 (2004)
JCR rank
31/259 (2004)
JCR quartile
1 (2004)
ISSN
0021-9258
DOI
10.1074/jbc.M406329200
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
298618
handle
http://hdl.handle.net/1854/LU-298618
date created
2005-02-11 13:11:00
date last changed
2013-10-17 16:03:35
@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 Inz{\'e}, Dirk and Van Breusegem, Frank},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keyword      = {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},
}

Chicago
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.
APA
Vercammen, D., Van De Cotte, B., De Jaeger, G., Eeckhout, D., Casteels, P., Vandepoele, K., Vandenberghe, I., et al. (2004). Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine. JOURNAL OF BIOLOGICAL CHEMISTRY, 279(44), 45329–45336.
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.
MLA
Vercammen, Dominique, Brigitte Van De Cotte, Geert De Jaeger, et al. “Type II Metacaspases Atmc4 and Atmc9 of Arabidopsis Thaliana Cleave Substrates After Arginine and Lysine.” JOURNAL OF BIOLOGICAL CHEMISTRY 279.44 (2004): 45329–45336. Print.