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Comparative Profile of Rubisco-interacting Proteins From Arabidopsis: Photosynthesis Under Cold Conditions

文献类型: 外文期刊

作者: An Bai-Yi 2 ; Liu Xiao-Yu 3 ; Tan Hua 4 ; Lin Wei-Hong 1 ; Sun Li-Wen 2 ;

作者机构: 1.Jilin Univ, Hosp 1, Changchun 130021, Peoples R China

2.Jilin Univ, Key Lab Mol Enzymol & Engn, Minist Educ, Changchun 130012, Peoples R China

3.Shijingshan Dist Ctr Dis Control & Prevent, Beijing 100043, Peoples R China

4.JAAS, Biotechnol Res Ctr, Changchun 130033, Peoples R China

关键词: Arabidopsis;cold stress;Rubisco-interacting proteins;photosynthesis

期刊名称:PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS ( 影响因子:0.351; 五年影响因子:0.272 )

ISSN: 1000-3282

年卷期: 2011 年 38 卷 5 期

页码:

收录情况: SCI

摘要: Rubisco (Ribulose 1, 5-bisphosphate carboxylase/oxygenase, EC 4.1.1.39) is crucial in biological circumstance fluctuation. Although disassembly of Rubisco after chill treatment has been reported in previous studies, there is only little known data on Rubisco interactive proteins involved in the disassembly process of Rubisco. Both repression of net photosynthesis rate and disassembly of Rubisco large subunits (Ru-L) have been investigated in the wild type, Arabidopsis thaliana (Col-0), treated at 4 degrees C for 4 h and 24 h together with their 24 h recoveries at 20 degrees C. Co-immunoprecipitation coupled with sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis and MALDI-TOF MS identification was used to explore Rubisco-interacting proteins. Five protein candidates were profiled. The identified AAA-type ATPase family and glycosyltransferase were determined crucial for Rubisco activity. It is also strongly correlated to cold acclimation. Results suggest that the disassembly of Rubisco might have been the main cause of photosynthesis rate reduction under chill conditions, rather than photosystem or biogenesis involvement.

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