Deletion of the carboxyl terminal of thioredoxin reductase C of Arabidopsis facilitates oligomerization

作者：Moon Jeong Chan; Park Seong Cheol; Shin Su Young; Jung Young Jun; Jung Ji Hyun; Choi Wonkyun; Jang Mi Kyeong; Lee Sang Yeol; Lee Jung Ro

来源：Biotechnology and Bioprocess Engineering, 2016, 21(5): 641-645.

DOI：10.1007/s12257-016-0390-3

• thioredoxin reductase
• antioxidant
• chaperone
• hydrophobicity
• peroxidase

The hydrophobicity of NADPH-thioredoxin reductase C (AtNTRC) of Arabidopsis was determined at the carboxyl terminal based on a Kyte-Dolittle hydropathy plot. A carboxyl-terminal deletion mutant of AtNTRC was made in this study to determine whether such deletion could affect the structure and function of AtNTRC. The mutant protein with 14 amino acids deleted at the carboxyl terminus (designated as AtNTRC Delta C14) was purified. It was found that AtNTRC Delta C14 protein had higher hydrophobicity compared to AtNTRC. Such increase in hydrophobicity of AtNTRC Delta C14 affected its native structure and functions. In addition, AtNTRC Delta C14 had higher number of high oligomeric complexes compared to AtNTRC based on native-gel electrophoresis and size exclusion chromatography. Although the chaperone activity of AtNTRC Delta C14 was enhanced, its NADPH-dependent reductase activity was lower compared to AtNTRC. Therefore, the hydrophobicity of the thioredoxin domain of AtNTRC is important for forming high molecular weight complexes and for maintaining functional balance between chaperone activity and thioredoxin reductase activity.

• 出版日期2016-9