Heat-shock and Redox-dependent Functional Switching of an H-type Arabidopsis Thioredoxin from a Disulfide Reductase to a Molecular Chaperone

Overview

Journal Plant Physiol

Specialty Physiology

Date 2009 Apr 3

PMID 19339505

Citations 45

Authors

Soo Kwon Park

Young Jun Jung

Jung Ro Lee

Young Mee Lee

Ho Hee Jang

Seung Sik Lee

Jin Ho Park

Sun Young Kim

Jeong Chan Moon

Sun Yong Lee

Ho Byoung Chae

Mi Rim Shin

Ji Hyun Jung

Min Gab Kim

Woe Yeon Kim

Dae-Jin Yun

Kyun Oh Lee

Sang Yeol Lee

Affiliations

Soon will be listed here.

Abstract

A large number of thioredoxins (Trxs), small redox proteins, have been identified from all living organisms. However, many of the physiological roles played by these proteins remain to be elucidated. We isolated a high M(r) (HMW) form of h-type Trx from the heat-treated cytosolic extracts of Arabidopsis (Arabidopsis thaliana) suspension cells and designated it as AtTrx-h3. Using bacterially expressed recombinant AtTrx-h3, we find that it forms various protein structures ranging from low and oligomeric protein species to HMW complexes. And the AtTrx-h3 performs dual functions, acting as a disulfide reductase and as a molecular chaperone, which are closely associated with its molecular structures. The disulfide reductase function is observed predominantly in the low M(r) forms, whereas the chaperone function predominates in the HMW complexes. The multimeric structures of AtTrx-h3 are regulated not only by heat shock but also by redox status. Two active cysteine residues in AtTrx-h3 are required for disulfide reductase activity, but not for chaperone function. AtTrx-h3 confers enhanced heat-shock tolerance in Arabidopsis, primarily through its chaperone function.

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