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Interactions of the DnaK (Hsp70) chaperone from Escherichia
coli with substrates are controlled by ATP. Nucleotide-induced
changes in DnaK conformation were investigated by monitoring changes in
tryptic digestion pattern and tryptophan fluorescence. Using
nucleotide-free DnaK preparations, not only the known ATP-induced major
changes in kinetics and pattern of proteolysis but also minor
ADP-induced changes were detected. Similar ATP-induced conformational
changes occurred in the DnaK-T199A mutant protein defective in ATPase
activity, demonstrating that they result from binding, not hydrolysis,
of ATP. N-terminal sequencing and immunological mapping of tryptic
fragments of DnaK identified cleavage sites that, upon ATP addition,
appeared within the proposed C-terminal substrate binding region and
disappeared in the N-terminal ATPase domain. They hence reflect
structural alterations in DnaK correlated to substrate release and
indicate ATP-dependent domain interactions. Domain interactions are a
prerequisite for efficient tryptic degradation as fragments of DnaK
comprising the ATPase and C-terminal domains were highly
protease-resistant. Fluorescence analysis of the N-terminally located
single tryptophan residue of DnaK revealed that the known ATP-induced
alteration of the emission spectrum, proposed to result directly from
conformational changes in the ATPase domain, requires the presence of
the C-terminal domain and therefore mainly results from altered domain
interaction. Analyses of the C-terminally truncated DnaK163 mutant
protein revealed that nucleotide-dependent interdomain communication
requires a 15-kDa segment assumed to constitute the substrate binding
site.
Volume 270,
Number 28,
Issue of July 14, pp. 16903-16910, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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