GrpE, a nucleotide exchange factor for DnaK

Harrison, Celia J.

doi:10.1379/1466-1268(2003)008<0218:ganeff>2.0.co;2

Cited by 110 publications

(92 citation statements)

References 50 publications

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“…The unfolded protein remains bound to DnaK-ADP until a favourable physiological state is regained. GrpE, in turn, functions as a nucleotide-exchange factor, and promotes dissociation of ADP from DnaK for ATP (Harrison, 2003;Liberek et al, 1991;McCarty et al, 1995;Winter & Jakob, 2004). Thus, all three proteins are essential for the DnaK system to be functional.…”

Section: Discussionmentioning

confidence: 99%

Role for dnaK locus in tolerance of multiple stresses in Staphylococcus aureus

et al. 2007

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Section: Discussionmentioning

confidence: 99%

Role for dnaK locus in tolerance of multiple stresses in Staphylococcus aureus

et al. 2007

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“…The chaperoning systems investigated were the molecular chaperone machine, chaperonins of group I, chaperonins of group II, prefoldins, and associated co-chaperones or co-factors (Macario and Conway de Macario 2001;Macario et al 2004). The molecular chaperone machine is essentially composed of three proteins, Hsp70(DnaK), Hsp40(DnaJ) (abbreviated DnaK and DnaJ, respectively), and GrpE in prokaryotes (Georgopoulos et al 1990;Bukau et al 2000;Harrison 2003), but in eukaryotes GrpE is replaced by other molecules (Alberti et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Evolution of a Protein-Folding Machine: Genomic and Evolutionary Analyses Reveal Three Lineages of the Archaeal hsp70(dnaK) Gene

et al. 2006

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Abstract. The stress chaperone protein Hsp70 (DnaK) (abbreviated DnaK) and its co-chaperones Hsp40(DnaJ) (or DnaJ) and GrpE are universal in bacteria and eukaryotes but occur only in some archaea clustered in the order 5¢-grpE-dnaK-dnaJ-3¢ in a locus termed Locus I. Three structural varieties of Locus I, termed Types I, II, and III, were identified, respectively, in Methanosarcinales, in Thermoplasmatales and Methanothermobacter thermoautotrophicus, and in Halobacteriales. These Locus I types corresponded to three groups identified by phylogenetic trees of archaeal DnaK proteins including the same archaeal subdivisions. These archaeal DnaK groups were not significantly interrelated, clustering instead with DnaKs from three bacterial lineages, Methanosarcinales with Firmicutes, Thermoplasmatales and M. thermoautotrophicus with Thermotoga, and Halobacteriales with Actinobacteria, suggesting that the three archaeal types of Locus I were acquired by independent events of lateral gene transfer. These associations, however, lacked strong bootstrap support and were sensitive to dataset choice and treereconstruction method. Structural features of dnaK loci in bacteria revealed that Methanosarcinales and Firmicutes shared a similar structure, also common to most other bacterial groups. Structural differences were observed instead in Thermotoga compared to Thermoplasmatales and M. thermoautotrophicus, and in Actinobacteria compared to Halobacteriales. It was also found that the association between the DnaK sequences from Halobacteriales and Actinobacteria likely reflects common biases in their amino acid compositions. Although the loci structural features and the DnaK trees suggested the possibility of lateral gene transfer between Firmicutes and Methanosarcinales, the similarity between the archaeal and the ancestral bacterial loci favors the more parsimonious hypothesis that all archaeal sequences originated from a unique prokaryotic ancestor.

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“…Nucleotide dissociation is a crucial step and therefore it is regulated by a variety of NEFs in eukaryotes. Four major NEF families in the cellular cytosol are classified as: GrpE-like, BAG proteins, HspBP1 and Hsp110 (Harrison, 2003;Kabani et al, 2002;Kabbage and Dickman, 2008;Shaner and Morano, 2007).…”

Section: Nucleotide Exchange Factors (Nefs)mentioning

confidence: 99%

Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle

Hartl

Bracher

2013

Nat Struct Mol Biol

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The Hsp70-interacting protein, Hip, cooperates with the chaperone Hsp70 in protein folding and prevention of aggregation. Hsp70 interacts with non-native protein substrates in an ATP-dependent reaction cycle regulated by J-domain proteins and nucleotide exchange factors (NEFs). Hip is thought to delay substrate release by slowing ADP dissociation from Hsp70. Here we present crystal structures of the dimerization domain and the tetratricopeptide repeat (TPR) domain of rat Hip. As shown in a cocrystal structure, the TPR core of Hip interacts with the Hsp70 ATPase domain through an extensive interface, to form a bracket that locks ADP in the binding cleft. Hip and NEF binding to Hsp70 are mutually exclusive, and thus Hip attenuates active cycling of Hsp70-substrate complexes. This mechanism explains how Hip enhances aggregation prevention by Hsp70 and facilitates transfer of specific proteins to downstream chaperones or the proteasome

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GrpE, a nucleotide exchange factor for DnaK

Cited by 110 publications

References 50 publications

Role for dnaK locus in tolerance of multiple stresses in Staphylococcus aureus

Role for dnaK locus in tolerance of multiple stresses in Staphylococcus aureus

Evolution of a Protein-Folding Machine: Genomic and Evolutionary Analyses Reveal Three Lineages of the Archaeal hsp70(dnaK) Gene

Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle

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