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Article

Enhancement of Chaperone Activity of Plant-Specific Thioredoxin through γ-Ray Mediated Conformational Change

by
Seung Sik Lee
1,†,
Hyun Suk Jung
2,†,
Soo-Kwon Park
3,
Eun Mi Lee
1,
Sudhir Singh
1,
Yuno Lee
4,
Kyun Oh Lee
4,
Sang Yeol Lee
4 and
Byung Yeoup Chung
1,*
1
Research Division for Biotechnology, Advanced Radiation Technology Institute (ARTI), Korea Atomic Energy Research Institute (KAERI), 29 Geumgu-gil, Jeongeup 580-185, Korea
2
Department of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon 200-701, Korea
3
Crop Foundation Division, National Institute of Crop Science, Rural Development Administration, 181 Hyeoksin-ro, Iseo-myeon, Wanju-gun 565-851, Korea
4
Division of Applied Life Science (Brain Korea 21 Program), Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Korea
*
Author to whom correspondence should be addressed.
†
These authors contributed equally to this work.
Int. J. Mol. Sci. 2015, 16(11), 27302-27312; https://doi.org/10.3390/ijms161126019
Submission received: 14 August 2015 / Revised: 1 October 2015 / Accepted: 23 October 2015 / Published: 13 November 2015
(This article belongs to the Section Biochemistry)
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Abstract

AtTDX, a thioredoxin-like plant-specific protein present in Arabidospis is a thermo-stable and multi-functional enzyme. This enzyme is known to act as a thioredoxin and as a molecular chaperone depending upon its oligomeric status. The present study examines the effects of γ-irradiation on the structural and functional changes of AtTDX. Holdase chaperone activity of AtTDX was increased and reached a maximum at 10 kGy of γ-irradiation and declined subsequently in a dose-dependent manner, together with no effect on foldase chaperone activity. However, thioredoxin activity decreased gradually with increasing irradiation. Electrophoresis and size exclusion chromatography analysis showed that AtTDX had a tendency to form high molecular weight (HMW) complexes after γ-irradiation and γ-ray-induced HMW complexes were tightly associated with a holdase chaperone activity. The hydrophobicity of AtTDX increased with an increase in irradiation dose till 20 kGy and thereafter decreased further. Analysis of the secondary structures of AtTDX using far UV-circular dichroism spectra revealed that the irradiation remarkably increased the exposure of β-sheets and random coils with a dramatic decrease in α-helices and turn elements in a dose-dependent manner. The data of the present study suggest that γ-irradiation may be a useful tool for increasing holdase chaperone activity without adversely affecting foldase chaperone activity of thioredoxin-like proteins.
Keywords: chaperone; γ-ray; protein; structural change; thioredoxin chaperone; γ-ray; protein; structural change; thioredoxin

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MDPI and ACS Style

Lee, S.S.; Jung, H.S.; Park, S.-K.; Lee, E.M.; Singh, S.; Lee, Y.; Lee, K.O.; Lee, S.Y.; Chung, B.Y. Enhancement of Chaperone Activity of Plant-Specific Thioredoxin through γ-Ray Mediated Conformational Change. Int. J. Mol. Sci. 2015, 16, 27302-27312. https://doi.org/10.3390/ijms161126019

AMA Style

Lee SS, Jung HS, Park S-K, Lee EM, Singh S, Lee Y, Lee KO, Lee SY, Chung BY. Enhancement of Chaperone Activity of Plant-Specific Thioredoxin through γ-Ray Mediated Conformational Change. International Journal of Molecular Sciences. 2015; 16(11):27302-27312. https://doi.org/10.3390/ijms161126019

Chicago/Turabian Style

Lee, Seung Sik, Hyun Suk Jung, Soo-Kwon Park, Eun Mi Lee, Sudhir Singh, Yuno Lee, Kyun Oh Lee, Sang Yeol Lee, and Byung Yeoup Chung. 2015. "Enhancement of Chaperone Activity of Plant-Specific Thioredoxin through γ-Ray Mediated Conformational Change" International Journal of Molecular Sciences 16, no. 11: 27302-27312. https://doi.org/10.3390/ijms161126019

APA Style

Lee, S. S., Jung, H. S., Park, S.-K., Lee, E. M., Singh, S., Lee, Y., Lee, K. O., Lee, S. Y., & Chung, B. Y. (2015). Enhancement of Chaperone Activity of Plant-Specific Thioredoxin through γ-Ray Mediated Conformational Change. International Journal of Molecular Sciences, 16(11), 27302-27312. https://doi.org/10.3390/ijms161126019

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