Plant Physiology Preview
Published on February 24, 2002; 10.1104/pp.010612
Received July 10, 2001
Returned for revision October 24, 2001
Accepted November 27, 2001
Changes in the Expression and the Enzymic Properties of the 20S
Proteasome in Sugar-Starved Maize Roots. Evidence for an in Vivo
Oxidation of the Proteasome
Gilles Basset , Philippe Raymond , Lada Malek , and and Renaud Brouquisse *
Unité de Physiologie Végétale, Institut National de la Recherche Agronomique, Centre de Recherche de Bordeaux, Boîte Postale 81, 33883 Villenave d'Ornon cedex, France (B.G., R.P., B.R.); and Department of Biology, Lakehead University, Thunder Bay, Ontario, Canada P7B 5E1 (M.L.)
* Corresponding author; email: brouquis{at}bordeaux.inra.fr.
The 20S proteasome (multicatalytic proteinase) was purified from maize (Zea mays L. cv DEA 1992) roots through a five-step procedure. After biochemical characterization, it was shown to be similar to most eukaryotic proteasomes. We investigated the involvement of the 20S proteasome in the response to carbon starvation in excised maize root tips. Using polyclonal antibodies, we showed that the amount of proteasome increased in 24-h-carbon-starved root tips compared with freshly excised tips, whereas the mRNA levels of  3 and ß6 subunits of 20S proteasome decreased. Moreover, in carbon-starved tissues, chymotrypsin-like and caseinolytic activities of the 20S proteasome were found to increase, whereas trypsin-like activities decreased. The measurement of specific activities and kinetic parameters of 20S proteasome purified from 24-h-starved root tips suggested that it was subjected to posttranslational modifications. Using dinitrophenylhydrazine, a carbonyl-specific reagent, we observed an increase in carbonyl residues in 20S proteasome purified from starved root tips. This means that 20S proteasome was oxidized during starvation treatment. Moreover, an in vitro mild oxidative treatment of 20S proteasome from non-starved material resulted in the activation of chymotrypsin-like, peptidyl-glutamyl-peptide hydrolase and caseinolytic-specific activities and in the inhibition of trypsin-like specific activities, similar to that observed for proteasome from starved root tips. Our results provide the first evidence for an in vivo carbonylation of the 20S proteasome. They suggest that sugar deprivation induces an oxidative stress, and that oxidized 20S proteasome could be associated to the degradation of oxidatively damaged proteins in carbon starvation situations.
This article has been cited by other articles:
|
|
|
|
 
A. Prins, P. D.R. van Heerden, E. Olmos, K. J. Kunert, and C. H. Foyer
Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) vesicular bodies
J. Exp. Bot.,
May 1, 2008;
59(7):
1935 - 1950.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
V. Jain, W. Kaiser, and S. C. Huber
Cytokinin Inhibits the Proteasome-Mediated Degradation of Carbonylated Proteins in Arabidopsis Leaves
Plant Cell Physiol.,
May 1, 2008;
49(5):
843 - 852.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Garmier, P. Priault, G. Vidal, S. Driscoll, R. Djebbar, M. Boccara, C. Mathieu, C. H. Foyer, and R. De Paepe
Light and Oxygen Are Not Required for Harpin-induced Cell Death
J. Biol. Chem.,
December 28, 2007;
282(52):
37556 - 37566.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Y. Xiong, A. L. Contento, P. Q. Nguyen, and D. C. Bassham
Degradation of Oxidized Proteins by Autophagy during Oxidative Stress in Arabidopsis
Plant Physiology,
January 1, 2007;
143(1):
291 - 299.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Kim, J.-W. Ahn, U.-H. Jin, D. Choi, K.-H. Paek, and H.-S. Pai
Activation of the Programmed Cell Death Pathway by Inhibition of Proteasome Function in Plants
J. Biol. Chem.,
May 23, 2003;
278(21):
19406 - 19415.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
