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Plant function and evolutionary biology
RESEARCH ARTICLE

Identification and characterisation of cold stress-related proteins in Oryza rufipogon at the seedling stage using label-free quantitative proteomic analysis

Li-Wei-Dan Bai A * , Jian Liu A * , Liang-Fang Dai A , Qian-Wen Deng A , Ya-Ling Chen A , Jian-Kun Xie A B and Xiang-Dong Luo https://orcid.org/0000-0001-6466-7144 A B
+ Author Affiliations
- Author Affiliations

A College of Life Science, Jiangxi Normal University, Nanchang 330022, PR China.

B Corresponding authors. Email: xdluolf@163.com; xiejiankun@yahoo.com

Functional Plant Biology 48(5) 542-555 https://doi.org/10.1071/FP20046
Submitted: 12 February 2020  Accepted: 15 December 2020   Published: 25 January 2021

Abstract

In this study, label-free quantitative proteomics were used to study cold stress-related proteins in Dongxiang wild rice (Oryza rufipogon Griff., DWR) and cold sensitive cultivated rice ‘Xieqingzao B’(Oryza sativa L. ssp. indica cv., XB). The results demonstrated the presence of 101 and 216 differentially expressed proteins (DEPs) were detected in DWR and XB, respectively, after cold stress. Bioinformatics analysis showed that DWR and XB differed significantly in their ability to scavenge reactive oxygen species (ROS) and regulate energy metabolism. Of the 101 DEPs of DWR, 46 DEPs related to differential expressed genes were also detected by transcriptome analysis. And 13 out of 101 DEPs were located in previous cold related quantitative trait loci (QTL). Quantitative real-time PCR analysis indicated that protein expression and transcription patterns were not similar in XB and DWR. Protein–protein interaction (PPI) network was constituted using the DEPs of DWR and XB, and the following three centre proteins were identified: Q8H3I3, Q9LDN2, and Q2QXR8. Next, we selected a centre protein and two of the 37 DEPs with high levels of differential expression (fold change ≥ 2) were used for cloning and prokaryotic expression. We found that Q5Z9Q8 could significantly improve the cold tolerance of Escherichia coli.

Keywords: cold tolerance, Dongxiang wild rice, label-free proteomics, protein–protein interaction.


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