Disease relevance of DOT5

• A double mutant (C107S/C112S) of nTPx overexpressed in Escherichia coli was spontaneously degraded upon freezing and thawing and its truncated form (residues 57-215; MW = 17837 Da) was crystallized with PEG 3350 and mercury(II) acetate as precipitants using the hanging-drop vapour-diffusion method [1].
• Hemolysate thioredoxin reductase and glutathione peroxidase activities correlate with serum selenium in a group of New Zealand men at high prostate cancer risk [2].

High impact information on DOT5

• In addition to the identification of Cys-106 as the primary catalytic site, these data suggest the formation of the intradisulfide bond as a part of the catalytic cycle between nTPx and thioredoxin. nTPx preferentially reduced alkyl-hydroperoxides rather than H2O2 [3].
• There are two cysteine residues in nTPx [3].
• Transcription of nTPx gene was induced in response to oxidative stress [3].
• It is a substrate for the NADPH-dependent thioredoxin reductase of rabbit bone marrow, catalyzes the reduction of insulin disulfides by dithiothreitol, and is a hydrogen donor for methionine sulfoxide reductase of yeast [4].
• The DOT5 gene was originally cloned as one of the DOT (disrupter of telomeric silencing) genes; and later it was re-discovered as a nuclear thioredoxin peroxidase in Saccharomyces cerevisiae [5].

Other interactions of DOT5

• Furthermore, Dot5 does not affect redox regulation of the Yap1 transcription factor [5].

References