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Reconsideration of an early dogma, saying “there is no evidence for disulfide bonds in proteins from archaea”

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Abstract

Stability and function of a large number of proteins are crucially dependent on the presence of disulfide bonds. Recent genome analysis has pointed out an important role of disulfide bonds for the structural stabilization of intracellular proteins from hyperthermophilic archaea and bacteria. These findings contradict the conventional view that disulfide bonds are rare in those proteins. A specific protein, known as protein disulfide oxidoreductase (PDO) is recognized as a potential key enzyme in intracellular disulfide-shuffling in hyperthermophiles. The structure of this protein consists of two combined thioredoxin-related units which together, in tandem-like manner, form a closed protein domain. Each of these units contains a distinct CXXC active site motif. Both sites seem to have different redox properties. A relation to eukaryotic protein disulfide isomerase is suggested by the observed structural and functional characteristics of the protein. Enzymological studies have revealed that both, the archaeal and bacterial forms of this protein show oxidative and reductive activity and are able to isomerize protein disulfides. The variety of active site disulfides found in PDO’s from hyperthermophiles is puzzling. It is assumed, that PDO enzymes in hyperthermophilic archaea and bacteria may be part of a complex system involved in the maintenance of protein disulfide bonds.

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Abbreviations

PDI:

Protein disulfide isomerase

PDO:

Protein disulfide oxido-reductase

DTT:

Dithiothreitol

GSH:

Reduced glutathione

GSSG:

Oxidized glutathione

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Authors and Affiliations

  1. Center of Structural Biochemistry, Karolinska Institutet NOVUM, 14157, Huddinge, Sweden

    Rudolf Ladenstein & Bin Ren

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  1. Rudolf Ladenstein
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  2. Bin Ren
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Correspondence to Rudolf Ladenstein.

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Communicated by D.A. Cowan.

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Ladenstein, R., Ren, B. Reconsideration of an early dogma, saying “there is no evidence for disulfide bonds in proteins from archaea”. Extremophiles 12, 29–38 (2008). https://doi.org/10.1007/s00792-007-0076-z

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