Plant Physiology 100:1486-1493 (1992)
© 1992 American Society of Plant Biologists
Environmental and Stress Physiology
Characterization of a Novel Protein Induced by Progressive or Rapid Drought and Salinity in Brassica napus Leaves 1
Marie-Pierre Reviron,
Nicole Vartanian,
Marc Sallantin,
Jean-Claude Huet,
Jean-Claude Pernollet and
Dominique de Vienne
Station de Génétique Végétale, Institut National de la Recherche Agronomique-Centre National de la Recherche Scientifique-Université Paris Sud, La Ferme du Moulon, 91190 Gif-sur-Yvette, France,
Institut des Sciences Végétales, Centre National de la Recherche Scientifique Unité Propre de Recherche 40, 91198 Gif-sur-Yvette Cedex, France,
Laboratoire d'Etude des Protéines, Institut National de la Recherche Agronomique, Route de St-Cyr, 78026 Versailles Cedex, France
Under progressive drought stress, Brassica napus displays differential leaf modifications. The oldest leaves, developed before the onset of water deficit, wilt gradually, whereas the youngest leaves harden. Hardening was distinguished by leaf turgor and bluish wax bloom when the shoot water potential was below 3 MPa and the leaf water saturation deficit was about 60%. This adaptive change was accompanied by modifications in two-dimensional protein profiles. Ten percent of the polypeptides had altered abundance or were unique to drought-stressed plants. Two-dimensional analysis of in vitro translation products did not reveal a general decrease in mRNA population. A 22-kD double polypeptide was increased by progressive or rapid water stress and salinity and disappeared upon rehydration. These polypeptides have a common N-terminal sequence, which does not reveal homology with any known water-stress protein but which contains the signature motif of soybean Künitz trypsin inhibitors. Immunoprecipitation allowed these polypeptides to be identified on two-dimensional gels of in vitro translation products. They appeared to be synthesized as a 24-kD precursor, and their transcript was present in the control well-watered leaves, where the polypeptides were never detected, indicating a possible translational regulation. A putative function of this protein, named BnD22, in the retardation of drought-induced leaf senescence is discussed.
1 This work was supported in part by grant No. 4561 from Action Incitative Programmée Institut National de la Recherche Agronomique.
This article has been cited by other articles:

|
 |

|
 |
 
M. Desclos, L. Dubousset, P. Etienne, F. Le Caherec, H. Satoh, J. Bonnefoy, A. Ourry, and J.-C. Avice
A Proteomic Profiling Approach to Reveal a Novel Role of Brassica napus Drought 22 kD/Water-Soluble Chlorophyll-Binding Protein in Young Leaves during Nitrogen Remobilization Induced by Stressful Conditions
Plant Physiology,
August 1, 2008;
147(4):
1830 - 1844.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
H. Satoh, A. Uchida, K. Nakayama, and M. Okada
Water-Soluble Chlorophyll Protein in Brassicaceae Plants is a Stress-Induced Chlorophyll-Binding Protein
Plant Cell Physiol.,
September 1, 2001;
42(9):
906 - 911.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
K. Sugihara, N. Hanagata, Z. Dubinsky, S. Baba, and I. Karube
Molecular Characterization of cDNA Encoding Oxygen Evolving Enhancer Protein 1 Increased by Salt Treatment in the Mangrove Bruguiera gymnorrhiza
Plant Cell Physiol.,
November 1, 2000;
41(11):
1279 - 1285.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
H. Satoh, K. Nakayama, and M. Okada
Molecular Cloning and Functional Expression of a Water-soluble Chlorophyll Protein, a Putative Carrier of Chlorophyll Molecules in Cauliflower
J. Biol. Chem.,
November 13, 1998;
273(46):
30568 - 30575.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. Riccardi, P. Gazeau, D. de Vienne, and M. Zivy
Protein Changes in Response to Progressive Water Deficit in Maize . Quantitative Variation and Polypeptide Identification
Plant Physiology,
August 1, 1998;
117(4):
1253 - 1263.
[Abstract]
[Full Text]
|
 |
|
|
|