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J. Biol. Chem., Vol. 277, Issue 41, 38468-38475, October 11, 2002
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From the Jules Stein Eye Institute, UCLA School of Medicine, Los
Angeles, California 90095
Hsp16.5, isolated from the hyperthermophilic
Archaea Methanococcus jannaschii, is a member of the
small heat-shock protein family. Small Hsps have 12- to 42-kDa
subunit sizes and have sequences that are conserved among all
organisms. The recently determined crystal structure of Hsp16.5
indicates that it consists discretely of 24 identical subunits. Using
fluorescence resonance energy transfer, we show that at temperatures
above 60 °C, the subunits of MjHsp16.5 freely and reversibly
exchange with a rate constant of exchange at 68 °C of
0.067min
Subunit Exchange, Conformational Stability, and Chaperone-like
Function of the Small Heat Shock Protein 16.5 from
Methanococcus jannaschii*
1. The subunit exchange reactions were strongly
temperature-dependent, similar to the exchange reactions of
the 
-crystallins. The exchange reaction was specific to MjHsp16.5
subunits, as other sHsps such as -crystallin were not structurally
compatible and could not integrate into the MjHsp16.5 oligomer. In
addition, we demonstrate that at temperatures as high as 70 °C,
MjHsp16.5 retains its multimeric structure and subunit organization.
Using insulin and -lactalbumin as model target proteins, we also
show that MjHsp16.5 at 37 °C is a markedly inefficient chaperone
compared with other sHsps with these substrates. The results of this
study support the hypothesis that MjHsp16.5 has a dynamic quaternary
structure at temperatures that are physiologically relevant to M. jannaschii.
*
This work was supported in part by National Eye Instititue
Grant R37-EY3897 (to J. H.) and by the Bank of America Giannini Foundation (to M. P. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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