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PMID:19293385

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Citation

Lee, JR, Lee, SS, Jang, HH, Lee, YM, Park, JH, Park, SC, Moon, JC, Park, SK, Kim, SY, Lee, SY, Chae, HB, Jung, YJ, Kim, WY, Shin, MR, Cheong, GW, Kim, MG, Kang, KR, Lee, KO, Yun, DJ and Lee, SY (2009) Heat-shock dependent oligomeric status alters the function of a plant-specific thioredoxin-like protein, AtTDX. Proc. Natl. Acad. Sci. U.S.A. 106:5978-83

Abstract

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.

Links

PubMed PMC2667072 Online version:10.1073/pnas.0811231106

Keywords

Arabidopsis Proteins/physiology; Dimerization; Heat-Shock Response/genetics; Molecular Chaperones; Molecular Weight; NADH, NADPH Oxidoreductases; Thioredoxins/physiology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ARATH:TDX

involved_in

GO:0010286: heat acclimation

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

ARATH:TDX

enables

GO:0016671: oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ARATH:TDX

involved_in

GO:0006457: protein folding

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ARATH:TDX

involved_in

GO:0051259: protein complex oligomerization

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ARATH:TDX

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8VWG7

F

Seeded From UniProt

complete


See also

References

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