Comparative proteomic analysis of apomictic monosomic addition line of Beta corolliflora and Beta vulgaris L. in sugar beet

2008 ◽  
Vol 36 (8) ◽  
pp. 2093-2098 ◽  
Author(s):  
Hong Zhu ◽  
Ying-Dong Bi ◽  
Li-Jie Yu ◽  
De-Dong Guo ◽  
Bai-Chen Wang
2009 ◽  
Vol 73 (2) ◽  
pp. 297-308 ◽  
Author(s):  
Haiying Li ◽  
Hongxiang Cao ◽  
Yuguang Wang ◽  
Qiuying Pang ◽  
Chunquan Ma ◽  
...  

2013 ◽  
Vol 12 (11) ◽  
pp. 4931-4950 ◽  
Author(s):  
Le Yang ◽  
Yanjun Zhang ◽  
Ning Zhu ◽  
Jin Koh ◽  
Chunquan Ma ◽  
...  

2012 ◽  
Vol 169 (9) ◽  
pp. 839-850 ◽  
Author(s):  
Le Yang ◽  
Chunquan Ma ◽  
Linlin Wang ◽  
Sixue Chen ◽  
Haiying Li

2015 ◽  
Vol 127 ◽  
pp. 18-33 ◽  
Author(s):  
Haiying Li ◽  
Yu Pan ◽  
Yongxue Zhang ◽  
Chuan Wu ◽  
Chunquan Ma ◽  
...  

2021 ◽  
Vol 62 (1) ◽  
Author(s):  
Jinna Li ◽  
Kun Wang ◽  
Meichao Ji ◽  
Tingyue Zhang ◽  
Chao Yang ◽  
...  

Abstract Background Salt stress is a major abiotic stress that limits plant growth, development and productivity. Studying the molecular mechanisms of salt stress tolerance may help to enhance crop productivity. Sugar beet monosomic addition line M14 exhibits tolerance to salt stress. Results In this work, the changes in the BvM14 proteome and redox proteome induced by salt stress were analyzed using a multiplex iodoTMTRAQ double labeling quantitative proteomics approach. A total of 80 proteins were differentially expressed under salt stress. Interestingly, A total of 48 redoxed peptides were identified for 42 potential redox-regulated proteins showed differential redox change under salt stress. A large proportion of the redox proteins were involved in photosynthesis, ROS homeostasis and other pathways. For example, ribulose bisphosphate carboxylase/oxygenase activase changed in its redox state after salt treatments. In addition, three redox proteins involved in regulation of ROS homeostasis were also changed in redox states. Transcription levels of eighteen differential proteins and redox proteins were profiled. (The proteomics data generated in this study have been submitted to the ProteomeXchange and can be accessed via username: [email protected], password: q9YNM1Pe and proteomeXchange# PXD027550.) Conclusions The results showed involvement of protein redox modifications in BvM14 salt stress response and revealed the short-term salt responsive mechanisms. The knowledge may inform marker-based breeding effort of sugar beet and other crops for stress resilience and high yield.


2016 ◽  
Vol 143 ◽  
pp. 286-297 ◽  
Author(s):  
Bing Yu ◽  
Jinna Li ◽  
Jin Koh ◽  
Craig Dufresne ◽  
Na Yang ◽  
...  

2021 ◽  
Author(s):  
Jinna Li ◽  
Meichao Ji ◽  
Tingyue Zhang ◽  
Chao Yang ◽  
He Liu ◽  
...  

Abstract Background: Salt stress is a major abiotic stress that limits plant growth, development and productivity. Studying the molecular mechanisms of salt stress tolerance may help to enhance crop productivity. Sugar beet monosomic addition line M14 exhibits tolerance to salt stress. Results: In this work, the changes in the BvM14 proteome and redox proteome induced by salt stress were analyzed using a multiplex iodoTMTRAQ double labeling quantitative proteomics approach. A total of 80 proteins were differentially expressed under salt stress. Interestingly, 42 potential redox-regulated proteins showed differential redox change under salt stress. A large proportion of the redox proteins were involved in photosynthesis, ROS homeostasis and other pathways. For example, ribulose bisphosphate carboxylase/oxygenase activase changed in its redox state after salt treatments. In addition, three redox proteins involved in regulation of ROS homeostasis were also changed in redox states. Transcription levels of eighteen differential proteins and redox proteins were profiled. Conclusions: The results showed involvement of protein redox modifications in BvM14 salt stress response and revealed the short-term salt responsive mechanisms. The knowledge may inform marker-based breeding effort of sugar beet and other crops for stress resilience and high yield.


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