title: A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities.
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 beta-sheets and three alpha-helices arranged in betaalphabetaalphabetabetaalpha, 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 degrees 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.
authors.affiliation: Structural Biology Center, Korea Institute of Science and Technology, P.O. Box 131, Cheongryang, Seoul, 130-650, Korea.
authors.forename: D Y
authors.initials: DY
authors.lastname: Lee
authors.forename: B Y
authors.initials: BY
authors.lastname: Ahn
authors.forename: K S
authors.initials: KS
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D017123:Bacteriophage T7 / Q000378:metabolism; D003001:Cloning, Molecular; D004220:Disulfides / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry; D054477:Glutaredoxins; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D017017:Methanococcus / Q000737:chemistry*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism; D011490:Protein Disulfide Reductase (Glutathione); D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D013880:Thioredoxin-Disulfide Reductase / Q000378:metabolism; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004220:Disulfides; D054477:Glutaredoxins; D007328:Insulin; D011506:Proteins; D011994:Recombinant Proteins; D013879:Thioredoxins; D010088:Oxidoreductases; D013880:Thioredoxin-Disulfide Reductase; D011490:Protein Disulfide Reductase (Glutathione)