Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes

Alderson, T. Reid; Kim, Jin Hae; Markley, John L.

doi:10.1016/j.str.2016.05.011

Cited by 92 publications

(87 citation statements)

References 124 publications

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“…Additionally, it was documented that in the thermotolerant L. edodes strain S606, the protein and transcript levels of LeDnaJ (LE01Gene01273) were significantly induced and up-regulated after heat stress (Fig 3b and 4d); this relationship between DnaJ and thermotolerance has rarely been reported in basidiomycetes. DnaJ proteins are important for protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of chaperone proteins Hsp70s [59,60]. Hsp42 required to maintain the solubility of various yeast proteins during heat shock was significantly up-regulated in the previous proteomic and transcriptomic analysis of HSR (heat shock response) [61].…”

Section: Hsps In Response To Heat Stressmentioning

confidence: 98%

Proteome and Transcriptome Reveal Involvement of Heat Shock Proteins and Indoleacetic Acid Metabolism Process in Lentinula Edodes Thermotolerance

Wang

Luo

et al. 2018

Cell Physiol Biochem

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Background/Aims: Heat stress could cause huge losses for Lentinula edodes in China and other Asian cultivation areas. Yet our understanding of mechanism how to defend to heat stress is incomplete. Methods: Using heat-tolerant and heat-sensitive strains of L. edodes, we reported a combined proteome and transcriptome analysis of L. edodes response to 40 °C heat stress for 24 h. Meanwhile, the effect of LeDnaJ on the thermotolerance and IAA (indoleacetic acid) biosynthesis in L. edodes was analyzed via the over-expression method. Results: The proteome results revealed that HSPs (heat shock proteins) such as Hsp40 (DnaJ), Hsp70, Hsp90 and key enzymes involved in tryptophan and IAA metabolism process LeTrpE, LeTrpD, LeTam-1, LeYUCCA were more highly expressed in S606 than in YS3357, demonstrating that HSPs and tryptophan as well as IAA metabolism pathway should play an important role in thermotolerance. Over-expression of LeDnaJ gene in S606 strains showed better tolerance to heat stress. It was also documented that intracellular IAA accumulation of S606 (8-fold up) was more than YS3357 (2-fold up), and exogenous IAA enhanced L. edodes tolerance to heat stress. Conclusion: Our data support the interest of LeTrpE, LeDnaJ, tryptophan and IAA could play a pivotal role in enhancing organism thermotolerance.

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Section: Hsps In Response To Heat Stressmentioning

confidence: 98%

Proteome and Transcriptome Reveal Involvement of Heat Shock Proteins and Indoleacetic Acid Metabolism Process in Lentinula Edodes Thermotolerance

Wang

Luo

et al. 2018

Cell Physiol Biochem

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“…Most eukaryotes, including humans, have a single multifunctional mitochondrial chaperone of the HSP70 family, which participates in diverse cellular functions by virtue of its ability to interact with an array of different J proteins (also known as HSP40s or co-chaperones) (for reviews, see 71, 112–114 ). Therefore, HSPA9, a human HSP70 family member, would have not been the ideal prey to use to screen the human proteome for potential interacting Fe-S proteins, due to its promiscuous ATP-dependent substrate binding recognition activity.…”

Section: Recent Progress: Identification Of Molecular Features That Gmentioning

confidence: 99%

Mammalian Fe–S proteins: definition of a consensus motif recognized by the co-chaperone HSC20

Maio

Rouault

2016

Metallomics

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Iron-sulfur (Fe-S) clusters are inorganic cofactors that are fundamental to several biological processes in all three kingdoms of life. In most organisms, Fe-S clusters are initially assembled on a scaffold protein, ISCU, and subsequently transferred to target proteins or to intermediate carriers by a dedicated chaperone/co-chaperone system. The delivery of assembled Fe-S clusters to recipient proteins is a crucial step in the biogenesis of Fe-S proteins, and, in mammals, it relies on the activity of a multiprotein transfer complex that contains the chaperone HSPA9, the co-chaperone HSC20 and the scaffold ISCU. How the transfer complex efficiently engages recipient Fe-S target proteins involves specific protein interactions that are not fully understood. This mini review focuses on recent insights into the molecular mechanism of amino acid motif recognition and discrimination by the co-chaperone HSC20, which guides Fe-S cluster delivery.

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“…Eukaryotic Hsp70 and its prokaryotic homolog, DnaK, are highly conserved proteins [24–27]. Hsp70/DnaK is comprised of an N-terminal nucleotide binding domain (NBD) and a C-terminal substrate-binding domain (SBD) that are connected by a flexible linker [25].…”

Section: Introductionmentioning

confidence: 99%

“…It collaborates with two cochaperones, an Hsp40 (J-domain protein) and a nucleotide exchange factor (NEF). The Hsp40 protein stimulates ATP hydrolysis by Hsp70/DnaK and presents substrate to Hsp70/DnaK while the NEF stimulates nucleotide exchange by Hsp70/DnaK [24, 27, 28]. …”

Section: Introductionmentioning

confidence: 99%

Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK

Kravats

Doyle

Hoskins

et al. 2017

Journal of Molecular Biology

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Hsp90 is a widely conserved and ubiquitous molecular chaperone that participates in ATP-dependent protein remodeling in both eukaryotes and prokaryotes. It functions in conjunction with Hsp70 and the Hsp70 cochaperones, an Hsp40 (J-protein) and a nucleotide exchange factor. In E. coli the functional collaboration between Hsp90Ec and Hsp70, DnaK, requires that the two chaperones directly interact. We used molecular docking to model the interaction of Hsp90Ec and DnaK. The top-ranked docked model predicted that a region in the nucleotide-binding domain of DnaK interacted with a region in the middle domain of Hsp90Ec. We then made substitution mutants in DnaK residues suggested by the model to interact with Hsp90Ec. Eleven of the twelve mutants tested were defective or partially defective in their ability to interact with Hsp90Ec in vivo in a bacterial two-hybrid assay and in vitro in a Bio-Layer Interferometry assay. These DnaK mutants were also defective in their ability to function collaboratively in protein remodeling with Hsp90Ec, but retained the ability to act with DnaK cochaperones. Taken together these results suggest that a specific region in the nucleotide-binding domain of DnaK is involved in the interaction with Hsp90Ec and this interaction is functionally important. Moreover, the region of DnaK that we found to be necessary for Hsp90Ec binding includes residues that are also involved in J-protein binding, suggesting a functional interplay between DnaK, DnaK cochaperones and Hsp90Ec.

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Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes

Cited by 92 publications

References 124 publications

Proteome and Transcriptome Reveal Involvement of Heat Shock Proteins and Indoleacetic Acid Metabolism Process in Lentinula Edodes Thermotolerance

Proteome and Transcriptome Reveal Involvement of Heat Shock Proteins and Indoleacetic Acid Metabolism Process in Lentinula Edodes Thermotolerance

Mammalian Fe–S proteins: definition of a consensus motif recognized by the co-chaperone HSC20

Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK

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