Abstract
Thermus thermophilus is an eubacteria that grows optimally at 75°C and was initially discovered in geothermal springs (1). Suprisingly, even though the proteins of this organism are constantly subjected to high temperatures and must therefore have evolved to be highly thermostable, this thermophilic bacteria expresses large amounts of heat-shock proteins (2-4). In addition, it was shown that the Hsp60 chaperonin of this organism can be induced by a small heat shock (80°C for 1 h). This thermophilic chaperonin has been cloned and overexpressed in Escherichia coli (3,4). The amino acid sequence of Hsp60 from T. thermophilus is highly homologous to the GroEL chaperonin from E. coli (52% identity) as shown in Fig. 1. It is similar to GroEL also in its structure, as seen by electron microscopy, in that it also comprises two rings of seven identical subunits (5-6). Each subunit has a mol-wt of approx 57 kDa, making the tetradecameric complex 800 kDa.
Sequence comparison of E. coli GroEL and Hsp60 from Thermus thermophilus. Identical residues are shaded.
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© 2000 Humana Press Inc.
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Quaite-Randall, E., Joachimiak, A. (2000). Purification of Hsp60 from Thermus thermophilus . In: Schneider, C. (eds) Chaperonin Protocols. Methods in Molecular Biology, vol 140. Humana, Totowa, NJ. https://doi.org/10.1385/1-59259-061-6:15
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DOI: https://doi.org/10.1385/1-59259-061-6:15
Publisher Name: Humana, Totowa, NJ
Print ISBN: 978-0-89603-739-7
Online ISBN: 978-1-59259-061-2
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