Crowding Modulates the Conformation, Affinity, and Activity of the Components of the Bacterial Disaggregase Machinery

Celaya, Garbiñe; Fernández-Higuero, José Ángel; Martín, Ianire; Rivas, Germán; Moro, Fernando; Muga, Arturo

doi:10.1016/j.jmb.2016.04.027

Cited by 3 publications

(2 citation statements)

References 57 publications

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“…DnaJ, also known as Hsp40, works as a chaperone and holdase that transfers unfolded, misfolded, or aggregated proteins to DnaK, stimulating the extended ADP-bound DnaK conformation that has high affinity for polypeptides and is endowed with foldase activity (16, 17). Although less efficient than DnaK, DnaJ can act independently as a foldase of denatured polypeptides (18).…”

Section: Resultsmentioning

confidence: 99%

DksA–DnaJ redox interactions provide a signal for the activation of bacterial RNA polymerase

Kim

Liu

Fitzsimmons

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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SignificanceTranscription in Gram-negative bacteria is greatly influenced by the synergistic interactions of DksA and the nucleotide alarmone guanosine tetraphosphate. Our investigations reveal a unique, previously unknown layer of transcriptional regulation that depends on redox-based protein–protein interactions between DksA and the molecular chaperone DnaJ. Tripartite connections between DksA, DnaJ, and guanosine tetraphosphate afford a dynamic range of transcriptional responses to H2O2 concentrations associated with redox signaling or oxidative stress. The redox-based gene regulation dependent on the combined actions of DksA, DnaJ, and guanosine tetraphosphate confers resistance of Salmonella to the antimicrobial activity of the NADPH phagocyte oxidase.

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Section: Resultsmentioning

confidence: 99%

DksA–DnaJ redox interactions provide a signal for the activation of bacterial RNA polymerase

Kim

Liu

Fitzsimmons

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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“…In yeast, such J-protein-mediated conglomerations of Hsp70 may aid in both efficient recruitment and activation of Hsp100 hexamers ( Seyffer et al, 2012 ; Carroni et al, 2014 ) on different aggregate types. To achieve a similar outcome, the bacterial disaggregase system seems to employ J-proteins with broad aggregate recognition and is proposed to rely on homo J-protein oligomerization ( Celaya et al, 2016 ). The precise basis of J-proteins binding to aggregates has not been defined, but presumably J-proteins nucleate where looped-out polypeptide stretches are available for interaction.…”

Section: Discussionmentioning

confidence: 99%

Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes

Nillegoda

Stank

Malinverni

et al. 2017

eLife

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Hsp70 participates in a broad spectrum of protein folding processes extending from nascent chain folding to protein disaggregation. This versatility in function is achieved through a diverse family of J-protein cochaperones that select substrates for Hsp70. Substrate selection is further tuned by transient complexation between different classes of J-proteins, which expands the range of protein aggregates targeted by metazoan Hsp70 for disaggregation. We assessed the prevalence and evolutionary conservation of J-protein complexation and cooperation in disaggregation. We find the emergence of a eukaryote-specific signature for interclass complexation of canonical J-proteins. Consistently, complexes exist in yeast and human cells, but not in bacteria, and correlate with cooperative action in disaggregation in vitro. Signature alterations exclude some J-proteins from networking, which ensures correct J-protein pairing, functional network integrity and J-protein specialization. This fundamental change in J-protein biology during the prokaryote-to-eukaryote transition allows for increased fine-tuning and broadening of Hsp70 function in eukaryotes.DOI: http://dx.doi.org/10.7554/eLife.24560.001

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Regulation of Human Hsc70 ATPase and Chaperone Activities by Apg2: Role of the Acidic Subdomain

Cabrera

Dublang

Fernández-Higuero

et al. 2019

Journal of Molecular Biology

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Crowding Modulates the Conformation, Affinity, and Activity of the Components of the Bacterial Disaggregase Machinery

Cited by 3 publications

References 57 publications

DksA–DnaJ redox interactions provide a signal for the activation of bacterial RNA polymerase

DksA–DnaJ redox interactions provide a signal for the activation of bacterial RNA polymerase

Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes

Regulation of Human Hsc70 ATPase and Chaperone Activities by Apg2: Role of the Acidic Subdomain

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