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Thermophilic Protein Folding Systems

  • Reference work entry
Extremophiles Handbook

Introduction

The study of adaptive stress responses was initiated at the molecular level with the observation of dramatic chromosome puffs coupled to the inducible transcription of specific proteins that were observed in Drosophila under heat stress (Ritossa 1962). Since then, stress responses have been observed in virtually all classes of organisms. Although a wide variety of survival strategies are deployed when cells are exposed to environmental challenges, such as heat stress, desiccation, chemical stress, or starvation, usually, the effector proteins are generically referred to as Heat Shock Proteins (HSPs). HSPs are diverse in structure and function, and are usually classified based on their subunit molecular weights. Classes that occur in microorganisms and in the majority of thermophiles include HSP100, HSP90, HSP70, HSP60, and the small HSPs (Trent 1996). Most of these proteins function as molecular chaperones, catalyzing the refolding of denatured proteins and assisting the...

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Authors and Affiliations

  1. Department of Microbiology and Immunology, University of Maryland, 701 E. Pratt Street, Baltimore, MD, 21202, USA

    Haibin Luo & Prof. Frank T. Robb

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  1. Haibin Luo
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  2. Prof. Frank T. Robb
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Correspondence to Frank T. Robb .

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Editors and Affiliations

  1. Extremobiosphere Research Center, Japan Agency for Marine-Earth Science and Technology (JAMSTEC) Yokohama, Professor Emeritus of Tokyo Institute of Technology, Tokyo, Japan

    Koki Horikoshi

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© 2011 Springer

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Luo, H., Robb, F.T. (2011). Thermophilic Protein Folding Systems. In: Horikoshi, K. (eds) Extremophiles Handbook. Springer, Tokyo. https://doi.org/10.1007/978-4-431-53898-1_27

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