A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities

Duck Yeon Lee, Byung Yoon Ahn, Key Sun Kim

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

A thioredoxin homologue (Mj0307) from the hyperthermophilic archaeon Methanococcus jannaschii (MjTRX) was cloned, produced in E. coli, and compared to the thioredoxin from E. coli (ETRX). The secondary structure profile of MjTRX obtained by NMR spectroscopy shows that it has four β- sheets and three α-helices arranged in βαβαββα, similar to that of glutaredoxin. However, MjTRX supports the growth of T7 bacteriophage in E. coli and is weakly reduced by the thioredoxin reductase from E. coli, indicating that MjTRX is functionally closer to a thioredoxin than a glutaredoxin. MjTRX has higher specific insulin reductase activity than ETRX and retained its full activity over 4 days at 95 °C, whereas ETRX lost its activity in 150 min. The standard state redox potential of MjTRX is about - 277 mV, which is the lowest value thus far known among redox potentials of the thioredoxin superfamily. This indicates that the lower redox potential is necessary in keeping catalytic disulfide bonds reduced in the cytoplasm and in coping with oxidative stress in an anaerobic hyperthermophile.

Original languageEnglish
Pages (from-to)6652-6659
Number of pages8
JournalBiochemistry
Volume39
Issue number22
DOIs
Publication statusPublished - 2000 Jun 6

ASJC Scopus subject areas

  • Biochemistry

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