Journal Article

A review of acquired thermotolerance, heat-shock proteins, and molecular chaperones in archaea

Jonathan D. Trent

in FEMS Microbiology Reviews

Volume 18, issue 2-3, pages 249-258
Published in print May 1996 |
Published online January 2006 | e-ISSN: 1574-6976 | DOI: http://dx.doi.org/10.1111/j.1574-6976.1996.tb00241.x

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Abstract

Acquired thermotolerance, the associated synthesis of heat-shock proteins (HSPs) under stress conditions, and the role of HSPs as molecular chaperones under normal growth conditions have been studied extensively in eukaryotes and bacteria, whereas research in these areas in archaea is only beginning. All organisms have evolved a variety of strategies for coping with high-temperature stress, and among these strategies is the increased synthesis of HSPs. The facts that both high temperatures and chemical stresses induce the HSPs and that some of the HSPs recognize and bind to unfolded proteins in vitro have led to the theory that the function of HSPs is to prevent protein aggregation in vivo. The facts that some HSPs are abundant under normal growth conditions and that they assist in protein folding in vitro have led to the theory that they assist protein folding in vivo; in this role, they are referred to as molecular chaperones. The limited research on acquired thermotolerance, HSPs, and molecular chaperones in archaea, particularly the hyperthermophilic archaea, suggests that these extremophiles provide a new perspective in these areas of research, both because they are members of a separate phylogenetic domain and because they have evolved to live under extreme conditions.

Keywords: Acquired thermotolerance; Heat shock protein; Molecular chaperone; Eukaryote; Bacteria; Archaea

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