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Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase

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Abstract

Protein disulfide oxidoreductases (PDOs) are proteins involved in disulfide bond formation playing a crucial role in adaptation to extreme environment. This paper reports the functional and structural characterization of Sso1120, a PDO from the hyperthermophilic archaeon Sulfolobus solfataricus. The protein was expressed in Escherichia coli and purified to homogeneity. The functional characterization showed that the enzyme has reductase activity, as tested by insulin assay, but differently from the other PDOs, it does not present isomerase activity. In addition it is able to form a redox couple with the thioredoxin reductase that could be used in undiscovered pathways. The protein revealed a melting point of around 90 °C in CD spectroscopy-monitored thermal denaturation and high denaturant resistance. The X-ray crystallographic structure was solved at 1.80 Å resolution, showing differences with respect to other PDOs and an unexpected similarity with the N-terminal domain of the alkyl hydroperoxide reductase F component from Salmonella typhimurium. On the basis of the reported data and of bioinformatics and phylogenetic analyses, a possible involvement of this atypical PDO in a new antioxidant system of S. solfataricus has been proposed.

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Acknowledgments

We gratefully acknowledge the support from MIUR for project FIRB no. RBRN07BMCT and Università Federico II per l’Avvio di Ricerche Originali (FARO 2011) CUP:E61J1200060005.

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Authors and Affiliations

  1. Dipartimento di Biologia, Università degli Studi di Napoli ‘‘Federico II’’, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126, Naples, Italy

    Danila Limauro, Simonetta Bartolucci & Emilia Pedone

  2. Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Naples, Italy

    Giuseppina De Simone, Katia D’Ambrosio & Emilia Pedone

  3. Istituto di Cristallografia, CNR, Via Giovanni Amendola 122/O, 70126, Bari, Italy

    Luciano Pirone

Authors
  1. Danila Limauro
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  2. Giuseppina De Simone
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  3. Luciano Pirone
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  4. Simonetta Bartolucci
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  5. Katia D’Ambrosio
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  6. Emilia Pedone
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Corresponding authors

Correspondence to Katia D’Ambrosio or Emilia Pedone.

Additional information

Communicated by S. Albers.

D. Limauro and G. De Simone contributed equally to this work.

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Limauro, D., De Simone, G., Pirone, L. et al. Sulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductase. Extremophiles 18, 219–228 (2014). https://doi.org/10.1007/s00792-013-0607-8

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  • DOI: https://doi.org/10.1007/s00792-013-0607-8

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