In vivo occurrence of carbonyl residues in Phaseolus vulgaris proteins as a direct consequence of a chronic ozone stress

被引:29
作者
Junqua, M [1 ]
Biolley, JP [1 ]
Pie, S [1 ]
Kanoun, M [1 ]
Duran, R [1 ]
Goulas, P [1 ]
机构
[1] Univ Pau & Pays Adour, IBEAS, Lab Ecol Mol, F-64013 Pau, France
关键词
carbonyl residue; ozone stress; Phaseolus vulgaris; protein oxidation; Rubisco; ribulose-1,5-biphosphate carboxylase; oxygenase;
D O I
10.1016/S0981-9428(00)01193-1
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
We aimed to show that a chronic and realistic ozone stress could induce in vivo formation of carbonyl groups in leaf proteins of bean (Phaseolus vulgaris L. cv Bergamo). Plants were grown in three open-top chambers with increasing ozone concentrations: non-filtered air (NF), NF+40 nL.L-1, NF+80 nL.L-1 ozone 7 h.d(-1) for 22 d. Carbonyl contents in proteins, evaluation of Rubisco (EC 4.1.1.39) amounts and visible damages were systematically investigated in primary and first trifoliate leaves. Visible ozone injuries clearly reflected the total external ozone dose (expressed as AOT40) that the leaf had suffered. Ozone was effective at inducing aldehydes and ketones formation in bean proteins. This production of carbonyl groups increased with ozone concentration, the most relevant difference being observed on the Rubisco small subunit (Rubisco SSU). Contrary to young first trifoliate leaves, older primary leaves from O-3-enriched atmospheres exhibited a two-fold decrease in Rubisco level. Carbonyl group formation in Rubisco SSU and decrease in Rubisco level were not necessarily linked. Depending on ozone concentration, exposure time and leaf age, these two effects were observed either together or separately for an almost similar external dose of ozone. To conclude, leaf symptoms, loss of Rubisco and oxidized Rubisco SSU could participate in the assessment of the impact of a chronic ozone stress. (C) 2000 Editions scientifiques et medicales Elsevier SAS.
引用
收藏
页码:853 / 861
页数:9
相关论文
共 28 条
[21]   Senescence-associated gene expression during ozone-induced leaf senescence in Arabidopsis [J].
Miller, JD ;
Arteca, RN ;
Pell, EJ .
PLANT PHYSIOLOGY, 1999, 120 (04) :1015-1023
[22]  
Nakamura A, 1996, J BIOCHEM, V119, P768
[23]   TIMING OF OZONE STRESS AND RESULTING STATUS OF RIBULOSE BISPHOSPHATE CARBOXYLASE OXYGENASE AND ASSOCIATED NET PHOTOSYNTHESIS [J].
PELL, EJ ;
ECKARDT, N ;
ENYEDI, AJ .
NEW PHYTOLOGIST, 1992, 120 (03) :397-405
[24]   INCREASED SUSCEPTIBILITY OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE TO PROTEOLYTIC DEGRADATION CAUSED BY OXIDATIVE TREATMENTS [J].
PENARRUBIA, L ;
MORENO, J .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1990, 281 (02) :319-323
[25]   DIFFERENTIAL SUSCEPTIBILITY OF PLASMA-PROTEINS TO OXIDATIVE MODIFICATION - EXAMINATION BY WESTERN-BLOT IMMUNOASSAY [J].
SHACTER, E ;
WILLIAMS, JA ;
LIM, M ;
LEVINE, RL .
FREE RADICAL BIOLOGY AND MEDICINE, 1994, 17 (05) :429-437
[26]  
STADTMAN ER, 1991, J BIOL CHEM, V266, P2005
[27]   PROTEIN OXIDATION AND AGING [J].
STADTMAN, ER .
SCIENCE, 1992, 257 (5074) :1220-1224
[28]   ELECTROPHORETIC TRANSFER OF PROTEINS FROM POLYACRYLAMIDE GELS TO NITROCELLULOSE SHEETS - PROCEDURE AND SOME APPLICATIONS [J].
TOWBIN, H ;
STAEHELIN, T ;
GORDON, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (09) :4350-4354