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• W2088890018 abstract "The genes coding for the Thermus thermophilus (Tth) homologues of the molecular chaperones DnaK and GrpE (DnaKTthand GrpETth) were cloned and expressed in Escherichia coli. The proteins were purified and their functional properties were assessed by equilibrium and transient kinetic methods. DnaKTthhas an intrinsic ATPase activity of 3×10−4s−1at 25°C and 10×10−4 s−1at 75°C under single turnover conditions. It binds the fluorescent nucleotide analogue N8-(4-N′-methylanthraniloylaminobutyl)-8-aminoadenosine 5′-diphosphate (MABA-ADP) with a dissociation constant (Kd) of 3 nM and ADP with aKdof 47 nM at 25°C. At 75°C the affinities are decreased fivefold to 15 nM (MABA-ADP) and 280 nM (ADP). The kinetic constants for two-step binding of MABA-ADP and of ADP to DnaKTthwere determined at 25°C and 75°C, respectively. GrpETthacts as a nucleotide-exchange factor on DnaKTthand accelerates the release of bound MABA-ADP significantly. This shows that the nucleotide-binding domain is functionally intact, and that the specific interaction of DnaKTthand GrpETthis mediating nucleotide exchange. A fluorescently labelled peptide that comprises a subsequence of the E. coli transcription factor σ32binds to nucleotide-free DnaKTthwith aKdof 4.9 μM. Displacement with unlabelled peptide yields a Kdof 5.0 μM for the unlabelled peptide. Thus the peptide-binding domain also appears to be functional. For the cellular chaperone function of DnaK, a coupling between nucleotide and peptide-binding domains is required. However, with DnaKTthin the ATP as well as in the ADP.Pi-state, peptide is bound and released within seconds. No correlation between ATP-binding or hydrolysis by DnaKTthand changes in the σ32peptide exchange rates could be detected. It thus appears that the DnaK system from Th. thermophilus has a different mechanism of coupling the nucleotide state to the fast and slow peptide exchange properties." @default.
• W2088890018 created "2016-06-24" @default.
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• W2088890018 date "1998-06-01" @default.
• W2088890018 modified "2023-09-23" @default.
• W2088890018 title "Functional properties of the molecular chaperone DnaK from Thermus thermophilus" @default.
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• W2088890018 doi "https://doi.org/10.1006/jmbi.1998.1816" @default.
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