Overexpression of SBPase enhances photosynthesis against high temperature stress in transgenic rice plants

被引:137
作者
Feng, Lingling [1 ]
Wang, Kun [1 ]
Li, Yang [1 ]
Tan, Yanping [1 ]
Kong, Jin [1 ]
Li, Hui [1 ]
Li, Yangsheng [1 ]
Zhu, Yingguo [1 ]
机构
[1] Wuhan Univ, Coll Life Sci, Key Lab MOE Plant Dev Biol, Wuhan 430072, Peoples R China
基金
中国国家自然科学基金;
关键词
overexpression; high temperature stress; photosynthesis; sedoheptulose-1,7-bisphosphatase; transgenic rice;
D O I
10.1007/s00299-006-0299-y
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Activity of the Calvin cycle enzyme sedoheptulose-1,7-bisphosphatase (SBPase) was increased by overexpression of a rice plants 9,311 (Oryza sativa L.) cDNA in rice plants zhonghua11 (Oryza sativa L.). The genetic engineering enabled the plants to accumulate SBPase in chloroplasts and resulted in enhanced tolerance to high temperature stress during growth of young seedlings. Moreover, CO2 assimilation of transgenic plants was significantly more tolerant to high temperature than that of wild-type plants. The analyses of chlorophyll fluorescence and the content and activation of SBPase indicated that the enhancement of photosynthesis to high temperature was not related to the function of photosystem II but to the content and activation of SBPase. Western blotting analyses showed that high temperature stress led to the association of SBPase with the thylakoid membranes from the stroma fractions. However, such an association was much more pronounced in wild-type plants than that in transgenic plants. The results in this study suggested that under high temperature stress, SBPase maintained the activation of ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) by preventing the sequestration of Rubisco activase to the thylakoid membranes from the soluble stroma fraction and thus enhanced the tolerance of CO2 assimilation to high temperature stress. The results suggested that overexpression of SBPase might be an effective method for enhancing high temperature tolerance of plants.
引用
收藏
页码:1635 / 1646
页数:12
相关论文
共 36 条
[1]   Decrease in phosphoribulokinase activity by antisense RNA in transgenic tobacco. Relationship between photosynthesis, growth, and allocation at different nitrogen levels [J].
Banks, FM ;
Driscoll, SP ;
Parry, MAJ ;
Lawlor, DW ;
Knight, JS ;
Gray, JC ;
Paul, MJ .
PLANT PHYSIOLOGY, 1999, 119 (03) :1125-1136
[2]   PHOTOSYNTHETIC RESPONSE AND ADAPTATION TO TEMPERATURE IN HIGHER-PLANTS [J].
BERRY, J ;
BJORKMAN, O .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1980, 31 :491-543
[3]   PLANT PRODUCTIVITY AND ENVIRONMENT [J].
BOYER, JS .
SCIENCE, 1982, 218 (4571) :443-448
[4]   The two forms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase differ in sensitivity to elevated temperature [J].
CraftsBrandner, SJ ;
vandeLoo, FJ ;
Salvucci, ME .
PLANT PHYSIOLOGY, 1997, 114 (02) :439-444
[5]  
DUNKLEY P R, 1979, Biochimica et Biophysica Acta, V545, P175, DOI 10.1016/0005-2728(79)90124-5
[6]   Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco [J].
Feller, U ;
Crafts-Brandner, SJ ;
Salvucci, ME .
PLANT PHYSIOLOGY, 1998, 116 (02) :539-546
[7]  
FROVA C, 1997, PHYS STRESS PLANTS, P31
[8]   CONTROL OF CO2 FIXATION - REGULATION OF SPINACH RIBULOSE-5-PHOSPHATE KINASE BY STROMAL METABOLITE LEVELS [J].
GARDEMANN, A ;
STITT, M ;
HELDT, HW .
BIOCHIMICA ET BIOPHYSICA ACTA, 1983, 722 (01) :51-60
[9]   Inhibition of photosynthesis by high temperature in oak (Quercus pubescens L.) leaves grown under natural conditions closely correlates with a reversible heat-dependent reduction of the activation state of ribulose-1,5-bisphosphate carboxylase/oxygenase [J].
Haldimann, P ;
Feller, U .
PLANT CELL AND ENVIRONMENT, 2004, 27 (09) :1169-1183
[10]   Reduced sedoheptulose-1,7-bisphosphatase levels in transgenic tobacco lead to decreased photosynthetic capacity and altered carbohydrate accumulation [J].
Harrison E.P. ;
Willingham N.M. ;
Lloyd J.C. ;
Raines C.A. .
Planta, 1997, 204 (1) :27-36