Next Article in Journal
Targeting Mitochondrial Function to Treat Quiescent Tumor Cells in Solid Tumors
Previous Article in Journal
Pluripotency Genes and Their Functions in the Normal and Aberrant Breast and Brain
Article Menu
Issue 11 (November) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2015, 16(11), 27302-27312; doi:10.3390/ijms161126019

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

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
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Gian-Pietro Di Sansebastiano
Received: 14 August 2015 / Revised: 1 October 2015 / Accepted: 23 October 2015 / Published: 13 November 2015
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
View Full-Text   |   Download PDF [1402 KB, uploaded 13 November 2015]   |  

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. View Full-Text
Keywords: chaperone; γ-ray; protein; structural change; thioredoxin chaperone; γ-ray; protein; structural change; thioredoxin
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

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.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top