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- W591955276 abstract "Hsp70 chaperones bind and release non-native proteins in a process that relies on allosteric signaling between the nucleotide binding domain (NBD) and substrate binding domain (SBD): ATP-binding/hydrolysis by the N-terminal NBD regulates the affinity of the SBD for substrates, and conversely, binding of substrates enhances the NBD ATPase activity Taking advantage of the phylogenetic prevalence of Hsp70s, we identified clusters of evolutionarily co-dependent residues in continuous structural pathways that suggest elements of an allosteric mechanism (R. Smock, J. Swain, W. Russ, R. Ranganathan, and L. Gierasch, submitted). We are testing the resulting model for allostery and interdomain docking using a complementary experimental approach. NMR study of a new stable construct of the DnaK SBD showed that the empty state is overall quite similar to the peptide-bound state (J. Swain, E. Schulz, and L. Gierasch, J. Biol. Chem., paper in press 11/7/05). Moreover, the chemical shifts of the DnaK SBD and the NBD do not change in a two-domain construct in the absence of ligands. Strikingly, ATP binding leads to a profound change in the SBD as well as the NBD. Thus, the two domains actively dock in the presence of ATP. We have discovered that an NBD construct retaining four conserved hydrophobic residues of the interdomain linker mimics the substrate-activated NBD, arguing that the linker mediates allosteric communication. All of our results are converging on a model for the elusive and essential mode of interaction and allosteric signal transmission between the two domains of Hsp70s. [Supported by NIH grant GM027616]" @default.
- W591955276 created "2016-06-24" @default.
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- W591955276 date "2006-03-01" @default.
- W591955276 modified "2023-09-27" @default.
- W591955276 title "A multipronged approach to the mechanism of allostery in Hsp70 chaperones" @default.
- W591955276 doi "https://doi.org/10.1096/fasebj.20.5.a964" @default.
- W591955276 hasPublicationYear "2006" @default.
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