Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 14, Pages 5978-5983Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0811231106
Keywords
disulfide reductase; foldase chaperone; holdase chaperone; functional switching; Yedox
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Funding
- Ministry of Education, Science, and Technology/Korea Science and Engineering Foundation [R15-2003-012-01001-0]
- World Class University Program [R32-10148]
- Crop Functional Genomic Frontier Grant [CG3313-1]
- Medical Research Center [R13-2005-012-01003-0]
- Korea Research Foundation [KRF-2007-359-C00022]
- BK21 Program of Korea
- National Research Council of Science & Technology (NST), Republic of Korea [523330-09] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2007-359-C00022] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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We found that Arabidopsis AtTDX, a heat-stable and plant-specific thioredoxin (Trx)-like protein, exhibits multiple functions, acting as a disulfide reductase, foldase chaperone, and holdase chaperone. The activity of AtTDX, which contains 3 tetratricopeptide repeat (TPR) domains and a Trx motif, depends on its oligomeric status. The disulfide reductase and foldase chaperone functions predominate when AtTDX occurs in the low molecular weight (LMW) form, whereas the holdase chaperone function predominates in the high molecular weight (HMW) complexes. Because deletion of the TPR domains results in a significant enhancement of AtTDX disulfide reductase activity and complete loss of the holdase chaperone function, our data suggest that the TPR domains of AtTDX block the active site of Trx and play a critical role in promoting the holdase chaperone function. The oligomerization status of AtTDX is reversibly regulated by heat shock, which causes a transition from LMW to HMW complexes with concomitant functional switching from a disulfide reductase and foldase chaperone to a holdase chaperone. Overexpression of AtTDX in Arabidopsis conferred enhanced heat shock resistance to plants, primarily via its holdase chaperone activity.
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