Email this article Molecular characterization and expression profiling of the phosphoenolpyruvate carboxylase genes in peanut (Arachis hypogaea L.)
- Authors: Pan L.1,2, Zhang J.1,2, Chen N.1, Chen M.1, Wang M.1, Wang T.1, Chi X.1, Yuan M.3, Wan Y.2, Yu S.1, Liu F.2
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Affiliations:
- Shandong Peanut Research Institute
- State Key Laboratory of Crop Biology, Shandong Key Laboratory of Crop Biology, College of Agronomic Sciences
- Xinjiang Agricultural University
- Issue: Vol 64, No 4 (2017)
- Pages: 576-587
- Section: Research Papers
- URL: https://journals.rcsi.science/1021-4437/article/view/179753
- DOI: https://doi.org/10.1134/S1021443717040100
- ID: 179753
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Abstract
Phosphoenolpyruvate carboxylase (PEPC) is a tightly controlled enzyme located at the core of plant carbohydrate metabolism. Plant PEPCs belong to a small multigene family encoding several plant-type PEPC genes, along with at least one distantly related bacterial-type PEPC gene. The PEPC genes have been intensively studied in Arabidopsis, but not in peanut (Arachis hypogaea L.). Previously, we isolated five PEPC genes (AhPEPC1, AhPEPC2, AhPEPC3, AhPEPC4 and AhPEPC5) from peanut. Here, due to the sequencing of the peanut genome, we analyzed the complexity of its PEPC gene family, including phylogenetic relationships, gene structure and chromosome mapping. The results showed that AhPEPC1, AhPEPC2, AhPEPC3 and AhPEPC4 encoded typical plant-type enzymes, while AhPEPC5 was a bacterial-type PEPC. The recombinant proteins of these genes were expressed in Escherichia coli, and the calculated molecular weights of the recombinant proteins were 110.8 kD (AhPEPC1), 110.7 kD (AhPEPC2), 110.3 kD (AhPEPC3), 110.8 kD (AhPEPC4), and 116.4 kD (AhPEPC5). The expression patterns of AhPEPC1-5 were analyzed under cold, salt and drought conditions. Our results indicated that the expression of AhPEPC3 was rapidly and substantially enhanced under abiotic stress, whereas the expression of AhPEPC1 and AhPEPC2 was slightly enhanced under certain stress conditions. Some genes were down-regulated in leaves under stress: AhPEPC1, AhPEPC4 and AhPEPC5 under salt stress and AhPEPC4 and AhPEPC5 under drought stress. These results suggest that peanut PEPC proteins may differ in their functions during acclimation to abiotic stresses.
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About the authors
L. Pan
Shandong Peanut Research Institute; State Key Laboratory of Crop Biology, Shandong Key Laboratory of Crop Biology, College of Agronomic Sciences
Email: shanlinyu2012@163.com
China, Qingdao, 266100; Tai’an, 271018
J. Zhang
Shandong Peanut Research Institute; State Key Laboratory of Crop Biology, Shandong Key Laboratory of Crop Biology, College of Agronomic Sciences
Email: shanlinyu2012@163.com
China, Qingdao, 266100; Tai’an, 271018
N. Chen
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
China, Qingdao, 266100
M. Chen
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
China, Qingdao, 266100
M. Wang
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
China, Qingdao, 266100
T. Wang
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
China, Qingdao, 266100
X. Chi
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
China, Qingdao, 266100
M. Yuan
Xinjiang Agricultural University
Email: shanlinyu2012@163.com
China, Urumqi, 830052
Y. Wan
State Key Laboratory of Crop Biology, Shandong Key Laboratory of Crop Biology, College of Agronomic Sciences
Email: shanlinyu2012@163.com
China, Tai’an, 271018
S. Yu
Shandong Peanut Research Institute
Author for correspondence.
Email: shanlinyu2012@163.com
China, Qingdao, 266100
F. Liu
State Key Laboratory of Crop Biology, Shandong Key Laboratory of Crop Biology, College of Agronomic Sciences
Email: shanlinyu2012@163.com
China, Tai’an, 271018
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