Abstract
Hsp60 from yeast is a close homolog of bacterial GroEL and located in the matrix of mitochondria. Yeast mitochondrial hsp60 is encoded by an essential gene and its expression is induced two- to threefold upon heat shock (1). Like its bacterial counterpart, hsp60 consists of 14 identical subunits of about 60 kDa that form a double-ring structure in yeast. The homolog from mammalian mitochondria has been found to be stable and functional as a 7 mer (2). The ATPase rate of yeast hsp60 based on protomer at 25°C is 2.5 min-1. ATP hydroloysis is reduced to approximately half of this value by the cochaperonin hsp10 that binds to hsp60 in the presence of adenosine nucleotide. Hsp60 mediates the refolding; of mammalian mitochondrial malate dehydrogenase in vitro (3).
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© 2000 Humana Press Inc.
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Dubaquié, Y., Looser, R., Rospert, S. (2000). Purification of Yeast Mitochondrial Hsp60. In: Schneider, C. (eds) Chaperonin Protocols. Methods in Molecular Biology, vol 140. Humana, Totowa, NJ. https://doi.org/10.1385/1-59259-061-6:139
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DOI: https://doi.org/10.1385/1-59259-061-6:139
Publisher Name: Humana, Totowa, NJ
Print ISBN: 978-0-89603-739-7
Online ISBN: 978-1-59259-061-2
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