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Metacaspase activity of Arabidopsis thaliana is regulated by S-nitrosylation of a critical cysteine residue

Beatrice Belenghi UGent, Maria C Romero-Puertas, Dominique Vercammen UGent, Anouk Brackenier UGent, Dirk Inzé UGent, Massimo Delledonne and Frank Van Breusegem UGent (2007) JOURNAL OF BIOLOGICAL CHEMISTRY. 282(2). p.1352-1358
abstract
Nitric oxide (NO) regulates a number of signaling functions in both animals and plants under several physiological and pathophysiological conditions. S-Nitrosylation linking a nitrosothiol on cysteine residues mediates NO signaling functions of a broad spectrum of mammalian proteins, including caspases, the main effectors of apoptosis. Metacaspases are suggested to be the ancestors of metazoan caspases, and plant metacaspases have previously been shown to be genuine cysteine proteases that autoprocess in a manner similar to that of caspases. We show that S-nitrosylation plays a central role in the regulation of the proteolytic activity of Arabidopsis thaliana metacaspase 9 (AtMC9) and hypothesize that this S-nitrosylation affects the cellular processes in which metacaspases are involved. We found that AtMC9 zymogens are S-nitrosylated at their active site cysteines in vivo and that this posttranslational modification suppresses both AtMC9 autoprocessing and proteolytic activity. However, the mature processed form is not prone to NO inhibition due to the presence of a second S-nitrosylation-insensitive cysteine that can replace the S-nitrosylated cysteine residue within the catalytic center of the processed AtMC9. This cysteine is absent in caspases and paracaspases but is conserved in all reported metacaspases.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
YEAST, DEATH, NO, PLAYS, PROTEINS, CASPASE-3, TRANSFORMATION, NITRIC-OXIDE, IDENTIFICATION
journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
J. Biol. Chem.
volume
282
issue
2
pages
1352 - 1358
Web of Science type
Article
Web of Science id
000243295200061
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
5.581 (2007)
JCR rank
40/260 (2007)
JCR quartile
1 (2007)
ISSN
0021-9258
DOI
10.1074/jbc.M608931200
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
409108
handle
http://hdl.handle.net/1854/LU-409108
date created
2008-05-15 15:07:00
date last changed
2013-10-18 15:06:17
@article{409108,
  abstract     = {Nitric oxide (NO) regulates a number of signaling functions in both animals and plants under several physiological and pathophysiological conditions. S-Nitrosylation linking a nitrosothiol on cysteine residues mediates NO signaling functions of a broad spectrum of mammalian proteins, including caspases, the main effectors of apoptosis. Metacaspases are suggested to be the ancestors of metazoan caspases, and plant metacaspases have previously been shown to be genuine cysteine proteases that autoprocess in a manner similar to that of caspases. We show that S-nitrosylation plays a central role in the regulation of the proteolytic activity of Arabidopsis thaliana metacaspase 9 (AtMC9) and hypothesize that this S-nitrosylation affects the cellular processes in which metacaspases are involved. We found that AtMC9 zymogens are S-nitrosylated at their active site cysteines in vivo and that this posttranslational modification suppresses both AtMC9 autoprocessing and proteolytic activity. However, the mature processed form is not prone to NO inhibition due to the presence of a second S-nitrosylation-insensitive cysteine that can replace the S-nitrosylated cysteine residue within the catalytic center of the processed AtMC9. This cysteine is absent in caspases and paracaspases but is conserved in all reported metacaspases.},
  author       = {Belenghi, Beatrice and Romero-Puertas, Maria C and Vercammen, Dominique and Brackenier, Anouk and Inz{\'e}, Dirk and Delledonne, Massimo and Van Breusegem, Frank},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keyword      = {YEAST,DEATH,NO,PLAYS,PROTEINS,CASPASE-3,TRANSFORMATION,NITRIC-OXIDE,IDENTIFICATION},
  language     = {eng},
  number       = {2},
  pages        = {1352--1358},
  title        = {Metacaspase activity of Arabidopsis thaliana is regulated by S-nitrosylation of a critical cysteine residue},
  url          = {http://dx.doi.org/10.1074/jbc.M608931200},
  volume       = {282},
  year         = {2007},
}

Chicago
Belenghi, Beatrice, Maria C Romero-Puertas, Dominique Vercammen, Anouk Brackenier, Dirk Inzé, Massimo Delledonne, and Frank Van Breusegem. 2007. “Metacaspase Activity of Arabidopsis Thaliana Is Regulated by S-nitrosylation of a Critical Cysteine Residue.” Journal of Biological Chemistry 282 (2): 1352–1358.
APA
Belenghi, B., Romero-Puertas, M. C., Vercammen, D., Brackenier, A., Inzé, D., Delledonne, M., & Van Breusegem, F. (2007). Metacaspase activity of Arabidopsis thaliana is regulated by S-nitrosylation of a critical cysteine residue. JOURNAL OF BIOLOGICAL CHEMISTRY, 282(2), 1352–1358.
Vancouver
1.
Belenghi B, Romero-Puertas MC, Vercammen D, Brackenier A, Inzé D, Delledonne M, et al. Metacaspase activity of Arabidopsis thaliana is regulated by S-nitrosylation of a critical cysteine residue. JOURNAL OF BIOLOGICAL CHEMISTRY. 2007;282(2):1352–8.
MLA
Belenghi, Beatrice, Maria C Romero-Puertas, Dominique Vercammen, et al. “Metacaspase Activity of Arabidopsis Thaliana Is Regulated by S-nitrosylation of a Critical Cysteine Residue.” JOURNAL OF BIOLOGICAL CHEMISTRY 282.2 (2007): 1352–1358. Print.