2012年3月29日 · DnaK, the major bacterial Hsp70, is one of the most abundant constitutively expressed and stress inducible chaperones in the E. coli cytosol. Yet it is not essential under nonstress conditions at intermediate temperature (Bukau and Walker, 1989).

Mycoplasma heat shock proteins include homologs of two of the most broadly conserved heat shock proteins, DnaK and GroEL. Both of these proteins are involved in protein folding functions and are essential for cell survival.

The DnaK (Hsp70), DnaJ, and GrpE heat shock proteins of Escherichia coli constitute a cellular chaperone system for protein folding. Substrate interactions are controlled by the ATPase activity of DnaK which itself is regulated by the nucleotide exchange factor GrpE.

2024年1月22日 · Here we report a cryo-EM analysis of GrpE bound to an intact Mtb DnaK, revealing an asymmetric 1:2 DnaK−GrpE complex. The GrpE dimer ratchets to modulate both DnaK nucleotide-binding domain and...

2024年11月3日 · We investigated the roles of the DnaK (Hsp70), DnaJ and GrpE chaperones of Escherichia coli in prevention and repair of thermally induced protein damage using firefly luciferase as a test substrate.

2022年6月16日 · Our results demonstrate that the initial DnaK response is largely dependent on protein synthesis rate but as the recombinantly expressed protein accumulates and homeostasis is approached the...

2012年3月29日 · Upon deletion of TF, DnaK interacts increasingly with ribosomal and other small, basic proteins, while its association with large multidomain proteins is reduced. DnaK also functions prominently in stabilizing proteins for subsequent folding by GroEL.

2022年3月3日 · DnaK is a highly conserved protein belonging to the heat-shock protein 70 family of molecular chaperones, which plays important roles as a moonlighting protein in various bacteria. In the present study, we identified the surface exposure of M. hyorhinis DnaK.

Here, we show that dnaK is present in 98.9% of bacterial genomes, and 6.4% of them possess two or more DnaK paralogs. We found that the duplication of dnaK is positively correlated with an increase in proteomic complexity (proteome size, number of domains).

2005年4月15日 · The molecular chaperone DnaK recognizes and binds substrate proteins via a stretch of seven amino acid residues that is usually only exposed in unfolded proteins. The binding kinetics are regulated by the nucleotide state of DnaK, which alternates between DnaK·ATP (fast exchange) and DnaK·ADP (slow exchange).