Enviar artigo por via de e-mail Molecular characterization and expression profiling of the phosphoenolpyruvate carboxylase genes in peanut (Arachis hypogaea L.)
- Autores: 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
-
Afiliações:
- Shandong Peanut Research Institute
- State Key Laboratory of Crop Biology, Shandong Key Laboratory of Crop Biology, College of Agronomic Sciences
- Xinjiang Agricultural University
- Edição: Volume 64, Nº 4 (2017)
- Páginas: 576-587
- Seção: Research Papers
- URL: https://journal-vniispk.ru/1021-4437/article/view/179753
- DOI: https://doi.org/10.1134/S1021443717040100
- ID: 179753
Citar
Acesso aberto
Acesso está concedido
Somente assinantes
Resumo
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.
Palavras-chave
Sobre autores
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
República Popular da 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
República Popular da China, Qingdao, 266100; Tai’an, 271018
N. Chen
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
República Popular da China, Qingdao, 266100
M. Chen
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
República Popular da China, Qingdao, 266100
M. Wang
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
República Popular da China, Qingdao, 266100
T. Wang
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
República Popular da China, Qingdao, 266100
X. Chi
Shandong Peanut Research Institute
Email: shanlinyu2012@163.com
República Popular da China, Qingdao, 266100
M. Yuan
Xinjiang Agricultural University
Email: shanlinyu2012@163.com
República Popular da 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
República Popular da China, Tai’an, 271018
S. Yu
Shandong Peanut Research Institute
Autor responsável pela correspondência
Email: shanlinyu2012@163.com
República Popular da 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
República Popular da China, Tai’an, 271018
Arquivos suplementares
