Characterisation of the components of the thioredoxin system in the archaeon Sulfolobus solfataricus.

Extremophiles : Life Under Extreme Conditions
Pasquale GrimaldiM Masullo

Abstract

The thioredoxin system is a redox machinery widely distributed in nature and involved in several cellular functions. It is constituted of thioredoxin reductase (Trx-B), its protein substrate thioredoxin (Trx-A) and NADPH. We have previously characterised a Trx-B from the hyperthermophile Sulfolobus solfataricus (SsTrx-B3) (Ruocco et al. in Biochimie 86:883-892, 2004). As in the genome of this archaeon, the gene coding for another Trx-B (SsTrx-B2) and for two Trx-A (SsTrx-A1, SsTrx-A2) have been putatively identified, these proteins were obtained as recombinant forms and characterised. SsTrx-B2, different from SsTrx-B3, did not elicit a thioredoxin reductase activity. S. solfataricus possessed only one Trx-B (SsTrx-B3), which had two thioredoxins (SsTrx-A1 and SsTrx-A2) as substrates. These latter showed a homodimeric structure and catalysed insulin reduction using either DTT or NADPH/SsTrx-B3 as electron donors. In addition, the electron transfer between SsTrx-B3 and either SsTrx-A1 or SsTrx-A2 was fully reversible, thus allowing the determination of the redox potential of the thioredoxin system in S. solfataricus. Among the two thioredoxins, SsTrx-A2 appeared slightly more active and stable than SsTrx-A1. These data, besides s...Continue Reading

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Citations

Dec 3, 2013·Extremophiles : Life Under Extreme Conditions·Zhen YanTakayoshi Wakagi
May 30, 2009·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Alessia RuggieroLuigi Vitagliano
Aug 13, 2014·The FEBS Journal·Addison C McCarver, Daniel J Lessner
Jul 14, 2010·Journal of Biomedicine & Biotechnology·Francesca CecereMaria Rosaria Ruocco
May 10, 2020·Antioxidants·Mamta Rawat, Julie A Maupin-Furlow

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