Analysis of Arabidopsis thioredoxin-h isotypes identifies discrete domains that confer specific structural and functional properties
- Authors
- Jung, Young Jun; Chi, Yong Hun; Chae, Ho Byoung; Shin, Mi Rim; Lee, Eun Seon; Cha, Joon-Yung; Paeng, Seol Ki; Lee, Yuno; Park, Jin Ho; Kim, Woe Yeon; Kang, Chang Ho; Lee, Kyun Oh; Lee, Keun Woo; Yun, Dae-Jin; Lee, Sang Yeol
- Issue Date
- 15-Nov-2013
- Publisher
- PORTLAND PRESS LTD
- Keywords
- Arabidopsis thaliana; disulfide reductase; heat-shock-resistance; molecular chaperone; thioredoxin h
- Citation
- BIOCHEMICAL JOURNAL, v.456, pp.13 - 24
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL JOURNAL
- Volume
- 456
- Start Page
- 13
- End Page
- 24
- URI
- https://scholarworks.bwise.kr/gnu/handle/sw.gnu/20369
- DOI
- 10.1042/BJ20130618
- ISSN
- 0264-6021
- Abstract
- Multiple isoforms of Arabidopsis thaliana h-type thioredoxins (AtTrx-hs) have distinct structural and functional specificities. AtTrx-h3 acts as both a disulfide reductase and as a molecular chaperone. We prepared five representative AtTrx-hs and compared their protein structures and disulfide reductase and molecular chaperone activities. AtTrx-h2 with an N-terminal extension exhibited distinct functional properties with respect to other AtTrx-hs. AtTrx-h2 formed low-molecular-mass structures and exhibited only disulfide reductase activity, whereas the other AtTrx-h isoforms formed high-molecular-mass complexes and displayed both disulfide reductase and molecular chaperone activities. The domains that determine the unique structural and functional properties of each AtTrx-hs protein were determined by constructing a domain-swap between the N- and C-terminal regions of AtTrx-h2 and AtTrx-h3 (designated AtTrx-h-2N3C and AtTrx-h-3N2C respectively), an N-terminal deletion mutant of AtTrx-h2 [AtTrx-h2-N(Delta 19)] and site-directed mutagenesis of AtTrx-h3. AtTrx-h2-N(Delta 19) and AtTrx-h-3N2C exhibited similar properties to those of AtTrx-h2, but AtTrx-h-2N3C behaved more like AtTrx-h3, suggesting that the structural and functional specificities of AtTrx-hs are determined by their C-terminal regions. Hydrophobicity profiling and molecular modelling revealed that Ala(100) and Ala(106) in AtTrx-h3 play critical roles in its structural and functional regulation. When these two residues in AtTrx-h3 were replaced with lysine, AtTrx-h3 functioned like AtTrx-h2. The chaperone function of AtTrx-hs conferred enhanced heat-shock-resistance on a thermosensitive trx1/2-null yeast mutant.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - ETC > Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.gnu.ac.kr/handle/sw.gnu/20369)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.