Selenite Assimilation into Formate Dehydrogenase H Depends on Thioredoxin Reductase in Escherichia coli

Takahata, Muneaki; Tamura, Takashi; Abe, Katsumasa; Mihara, Hisaaki; Kurokawa, Shu; Yamamoto, Yoshihiro; Nakano, Ryohei; Esaki, Nobuyoshi; Inagaki, Kenji

doi:10.1093/jb/mvm247

Cited by 24 publications

(13 citation statements)

References 35 publications

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“…Interestingly, when measured at 30°C, WT performed better than at 37°C. This fact, however, was expected and essentially repeated the result of a previous study (15). All other variants followed the same pattern, having a higher activity at 30°C than at 37°C.…”

Section: Thermal Stability Of Trnasupporting

confidence: 87%

The Long D-stem of the Selenocysteine tRNA Provides Resilience at the Expense of Maximal Function

Ishii

Kotlova

Tapsoba

et al. 2013

Journal of Biological Chemistry

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Background:The selenocysteine tRNA (tRNA Sec ) has a uniquely long D-stem containing 6 base pairs. Results: The extended D-stem is not essential for function but is required for stability. Conclusion: Enhanced secondary structure in selenocysteine tRNA compensates for the absence of canonical tertiary interactions. Significance: The flexibility due to the absence of tertiary interactions is required for tRNA Sec function, whereas the enhanced secondary structure compensates for the decreased stability.

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Section: Thermal Stability Of Trnasupporting

confidence: 87%

The Long D-stem of the Selenocysteine tRNA Provides Resilience at the Expense of Maximal Function

Ishii

Kotlova

Tapsoba

et al. 2013

Journal of Biological Chemistry

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“…The wild-type MC4100 strain and a glutathione reductase knockout (gor::tet) mutant produced FDH-H activity and incorporated 75 Se-labeled selenite into the polypeptide of FDH-H, whereas the thioredoxin reductase knockout (trxB::kan) strain failed to incorporate it into the bacterial selenoprotein. 14) This suggests that reduction of selenite in vivo depends on the thioredoxin-reducing system, but the mechanism of trxB-dependent selenite assimilation is not clearly understood.…”

Section: àmentioning

confidence: 99%

Selenite Reduction by the Thioredoxin System: Kinetics and Identification of Protein-Bound Selenide

Tamura

Sato

Komori

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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Selenite (SeO(3)(2-)) assimilation into a bacterial selenoprotein depends on thioredoxin (trx) reductase in Esherichia coli, but the molecular mechanism has not been elucidated. The mineral-oil overlay method made it possible to carry out anaerobic enzyme assay, which demonstrated an initial lag-phase followed by time-dependent steady NADPH consumption with a positive cooperativity toward selenite and trx. SDS-PAGE/autoradiography using (75)Se-labeled selenite as substrate revealed the formation of trx-bound selenium in the reaction mixture. The protein-bound selenium has metabolic significance in being stabilized in the divalent state, and it also produced the selenopersulfide (-S-SeH) form by the catalysis of E. coli trx reductase (TrxB).

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“…In E. coli the system mediates iron binding and delivery, has chaperone and protein disulfide isomerase activities, reduces glutaredoxin, and is involved in the reductive assimilation of selenite [9][10][11][12][13]. In the bacterium Helicobacter pylori, thioredoxin acts as an arginase chaperone capable of re-naturing the enzyme to a catalytically active state [14].…”

Section: The Thioredoxin Systemmentioning

confidence: 99%

Inhibition of Disulfide Reductases as a Therapeutic Strategy

Kaakoush¹,

Mendz

2009

CEI

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Disulfide reductases are involved in many functions in the cell, in particular, maintaining the intracellular redox balance. Many classes of these enzymes exist, and their inhibition has served as an effective therapy against different types of human diseases. The involvement of disulfide reductases in various cellular processes is reviewed, and therapeutic strategies against pathogenic bacteria, parasitic infections, and human diseases based on their inhibition are discussed.

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Selenite Assimilation into Formate Dehydrogenase H Depends on Thioredoxin Reductase in Escherichia coli

Cited by 24 publications

References 35 publications

The Long D-stem of the Selenocysteine tRNA Provides Resilience at the Expense of Maximal Function

The Long D-stem of the Selenocysteine tRNA Provides Resilience at the Expense of Maximal Function

Selenite Reduction by the Thioredoxin System: Kinetics and Identification of Protein-Bound Selenide

Inhibition of Disulfide Reductases as a Therapeutic Strategy

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