Proteomic analysis of grapevine (Vitis vinifera L.) tissues subjected to herbicide stress

被引:77
作者
Castro, AJ
Carapito, C
Zorn, N
Magné, C
Leize, E
Van Dorsselaer, A
Clément, C
机构
[1] Univ Reims, Lab Stress Def & Reprod Plantes, URVVC, UPRES EA 2069,UFR Sci, F-51687 Reims, France
[2] ULP, CNRS, UMR 7509, Ecole Europeenne Chim Polymeres & Mat,Lab Spectro, F-67087 Strasbourg, France
关键词
De novo sequencing; flumioxazin; grapevine; herbicide stress; PRP-10; two-dimensional electrophoresis;
D O I
10.1093/jxb/eri271
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Two-dimensional gel electrophoresis coupled to mass spectrometry analysis was used to examine for the first time the effect of a herbicide (flumioxazin) on a crop species (Vitis vinifera L.) at the proteome level. Examination of 2-D maps derived from chemically stressed tissues revealed the presence of 33 spots displaying a differential expression pattern. The presence of stress responsive proteins in the different plant organs analysed suggests that flumioxazin could act systemically. Among the responsive proteins, some photosynthesis-related proteins, including several fragments of the enzyme Rubisco, were identified. This effect suggests that photosynthesis could be impaired by the herbicide. The induction of several enzymatic antioxidant systems was also observed, probably as a result of an oxidative stress. Moreover, the photorespiration pathway was stimulated, as suggested by the induction of some key enzymes involved in this process. Changes in carbon metabolism-associated proteins presumably reflect altered patterns of carbon flux in response to impaired photosynthesis and an increased need for osmotic adjustment in affected tissues. Finally, plant defences were stimulated as revealed by the induction of a set of proteins belonging to the pathogenesis-related 10 class, suggesting that they could play an essential role in cell defence mechanisms against flumioxazin.
引用
收藏
页码:2783 / 2795
页数:13
相关论文
共 58 条
[1]  
Agarwal GK, 2002, PROTEOMICS, V2, P947, DOI 10.1002/1615-9861(200208)2:8<947::AID-PROT947>3.0.CO
[2]  
2-J
[3]   The grand design of photosynthesis: Acclimation of the photosynthetic apparatus to environmental cues [J].
Anderson, JM ;
Chow, WS ;
Park, YI .
PHOTOSYNTHESIS RESEARCH, 1995, 46 (1-2) :129-139
[4]   A 2-DIMENSIONAL GEL DATABASE OF RAT-LIVER PROTEINS USEFUL IN GENE-REGULATION AND DRUG EFFECTS STUDIES [J].
ANDERSON, NL ;
ESQUERBLASCO, R ;
HOFMANN, JP ;
ANDERSON, NG .
ELECTROPHORESIS, 1991, 12 (11) :907-930
[5]   ASCORBATE PEROXIDASE - A HYDROGEN PEROXIDE-SCAVENGING ENZYME IN PLANTS [J].
ASADA, K .
PHYSIOLOGIA PLANTARUM, 1992, 85 (02) :235-241
[6]   Direct evidence for ribonucleolytic activity of a PR-10-like protein from white lupin roots [J].
Bantignies, B ;
Séguin, J ;
Muzac, I ;
Dédaldéchamp, F ;
Gulick, P ;
Ibrahim, R .
PLANT MOLECULAR BIOLOGY, 2000, 42 (06) :871-881
[7]   Crystal structures of two homologous pathogenesis-related proteins from yellow lupine [J].
Biesiadka, J ;
Bujacz, G ;
Sikorski, MM ;
Jaskolski, M .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 319 (05) :1223-1234
[8]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[9]  
Bufe A, 1996, PLANTA, V199, P413, DOI 10.1007/BF00195733
[10]   Patterns of protein synthesis and tolerance of anoxia in root tips of maize seedlings acclimated to a low-oxygen environment, and identification of proteins by mass spectrometry [J].
Chang, WWP ;
Huang, L ;
Shen, M ;
Webster, C ;
Burlingame, AL ;
Roberts, JKM .
PLANT PHYSIOLOGY, 2000, 122 (02) :295-317