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Structure, Function and Evolution of the Hsp60 Chaperonins

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Prokaryotic Chaperonins

Part of the book series: Heat Shock Proteins ((HESP,volume 11))

Abstract

In 1973, Christian Anfinsen and coworkers noted that accelerated protein folding in intact cells and cell extracts suggested that a “disulfide interchange enzyme” might be present in vivo. This concept of catalyzed folding foreshadowed the discovery of ubiquitous protein chaperones. The chaperonin GroEL/GroES was identified serendipitously when GroE mutants of E. coli failed to grow bacteriophage λ and were also temperature sensitive. The GroEL/GroES proved to be a ubiquitous chaperone and heat shock protein in bacteria and eukaryotic organelles, with two back-to-back rings of seven subunits each, forming a cavity that enclosed nonnative proteins, capped by the separate GroES lid complex. Group II chaperonins were subsequently discovered in all of the Archaea and in the Eukaryote cytoplasm with a similar cage-like shape, only with a “built-in” lid instead of the GroES module of Group I chaperonins. These chaperones have been intensely studied for three decades and have provided deep insights into protein-folding mechanisms. Despite this, some aspects of chaperonin-induced protein folding remain controversial.

The shared architecture and sequence similarity of two classes of chaperonins implies that they share a common ancestor. A recently identified, deeply branching clade of archaeal-like chaperonins encoded in bacteria may shed light on the early history of chaperonins. This clade shares many molecular properties with Group II chaperones; however, their phylogeny suggests that they arose early in prokaryotic evolution and may represent a vestige of the common ancestor of Group I and Group II chaperonins.

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  1. Department of Microbiology and Immunology, School of Medicine, University of Maryland, Baltimore, and Institute of Marine and Environmental Technology (IMET), Columbus Center, Baltimore, MD, USA

    Sara E. Rowland & Frank T. Robb

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  1. Sara E. Rowland
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  2. Frank T. Robb
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Correspondence to Frank T. Robb .

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  1. Institute of Microbiology and Infection – School of Biosciences, University of Birmingham, Birmingham, West Midlands, United Kingdom

    C. M. Santosh Kumar

  2. Laboratory of Structural Biology, National Centre for Cell Science, Pune, Maharashtra, India

    Shekhar C. Mande

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© 2017 Springer Nature Singapore Pte Ltd.

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Rowland, S.E., Robb, F.T. (2017). Structure, Function and Evolution of the Hsp60 Chaperonins. In: Kumar, C., Mande, S. (eds) Prokaryotic Chaperonins. Heat Shock Proteins, vol 11. Springer, Singapore. https://doi.org/10.1007/978-981-10-4651-3_1

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