Lee, DY Ahn, BY Kim, KS 2024-01-21T14:03:52Z 2024-01-21T14:03:52Z 2021-09-04 2000-06 0006-2960 https://pubs.kist.re.kr/handle/201004/141363 A thioredoxin homologue (Mj0307) from the hyperthermophilic archaeon Methanococcus jannaschii (MjTRX) was cloned, produced in E. coli, and compared to the thioredoxin fr-om E. coli (ETRX). The secondary structure profile of MjTRX obtained by NMR spectroscopy shows that it has four beta-sheets and three a-helices arranged in beta alpha beta alpha beta beta alpha, 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. English AMER CHEMICAL SOC A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities Article 10.1021/bi000035b 1 BIOCHEMISTRY, v.39, no.22, pp.6652 - 6659 BIOCHEMISTRY 39 22 6652 6659 N scie scopus 000087580500009 2-s2.0-0001356912 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article ESCHERICHIA-COLI THIOREDOXIN DISULFIDE BOND FORMATION BACTERIOPHAGE-T7 DNA-POLYMERASE ACID REPLICATION INVITRO COMPLETE GENOME SEQUENCE SITE CYSTEINE RESIDUES T7 DEOXYRIBONUCLEIC-ACID ACTIVE-SITE REDOX PROPERTIES FILAMENTOUS BACTERIOPHAGE thioredoxin