The oligomeric plasticity of Hsp20 of Sulfolobus acidocaldarius protects environment-induced protein aggregation and membrane destabilization

Roy, Mousam; Gupta, Sayandeep; Patranabis, Somi; Ghosh, Abhrajyoti

doi:10.1016/j.bbamem.2018.09.005

Cited by 21 publications

(34 citation statements)

References 81 publications

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“…In contrast, sHSPs have no intrinsic refolding abilities themselves. However, in the presence of denaturing proteins, the sHSP-1 oligomer of Sulfolobus acidocaldarius undergoes dissociation into an active dimeric form that acts as a molecular 'trap' for unfolded proteins thereby preventing them from aggregation (Laksanalamai & Robb, 2004;Kocabiyik et al, 2009;Roy et al, 2018). In addition, sHSP-1 stabilizes membrane lipids, counteracting the effect of temperature on membrane permeability (Roy et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

“…However, in the presence of denaturing proteins, the sHSP-1 oligomer of Sulfolobus acidocaldarius undergoes dissociation into an active dimeric form that acts as a molecular 'trap' for unfolded proteins thereby preventing them from aggregation (Laksanalamai & Robb, 2004;Kocabiyik et al, 2009;Roy et al, 2018). In addition, sHSP-1 stabilizes membrane lipids, counteracting the effect of temperature on membrane permeability (Roy et al, 2018). Similar to sHSPs, PFDs are ATP-independent chaperones that bind a large variety of denaturing proteins and typically transfer these to the thermosome complex for refolding (Vainberg et al, 1998;Siegert et al, 2000;Okochi et al, 2004;D'Amaro et al, 2008;Ohtaki et al, 2010;Sahlan et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

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Defining heat shock response for the thermoacidophilic model crenarchaeon Sulfolobus acidocaldarius

et al. 2020

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Defining heat shock response for the thermoacidophilic model crenarchaeon Sulfolobus acidocaldarius

et al. 2020

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“…This was determined by measuring the leakage of the fluorescent molecule 1,6-diphenylhexatriene (DPH) in the presence and absence of Hsp20. According to these findings, the presence of heat shock proteins in archaeosomes of S. acidocaldarius has an important impact on acid tolerance, as well as temperature related effects in regards to the membrane characterization and packed protein [95].…”

Section: Phmentioning

confidence: 94%

“…This leads to the proposal that other factors, such as media composition, also play a role in the coping mechanisms of Sulfolobales towards pH stress [94]. In addition, the presence of proteins, in particular heat shock protein 20 (Hsp20), can prevent stress-induced protein aggregation and membrane destabilization in archaeosomes [95]. Secretory vesicles and thus archaeosomes are unable to perform pH homeostasis, necessary for maintaining a neutral intrinsic pH.…”

Section: Phmentioning

confidence: 99%

The Cell Membrane of Sulfolobus spp.—Homeoviscous Adaption and Biotechnological Applications

Rastädter

Wurm

Spadiut

et al. 2020

IJMS

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The microbial cell membrane is affected by physicochemical parameters, such as temperature and pH, but also by the specific growth rate of the host organism. Homeoviscous adaption describes the process of maintaining membrane fluidity and permeability throughout these environmental changes. Archaea, and thereby, Sulfolobus spp. exhibit a unique lipid composition of ether lipids, which are altered in regard to the ratio of diether to tetraether lipids, number of cyclopentane rings and type of head groups, as a coping mechanism against environmental changes. The main biotechnological application of the membrane lipids of Sulfolobus spp. are so called archaeosomes. Archaeosomes are liposomes which are fully or partly generated from archaeal lipids and harbor the potential to be used as drug delivery systems for vaccines, proteins, peptides and nucleic acids. This review summarizes the influence of environmental parameters on the cell membrane of Sulfolobus spp. and the biotechnological applications of their membrane lipids.

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“…Like Hsp20 [20], both temperature and hydrophobicity play a crucial role in the functionality of Hsp14. More importantly, these two sHsps can form temperaturedependent hetero-oligomeric complexes by exchanging subunits.…”

Section: Introductionmentioning

confidence: 99%

Archaeal Hsp14 drives substrate shuttling between small heat shock proteins and thermosome: insights into a novel substrate transfer pathway

et al. 2021

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Heat shock proteins maintain protein homeostasis and facilitate the survival of an organism under stress. Archaeal heat shock machinery usually consists of only sHsps, Hsp70, and Hsp60. Moreover, Hsp70 is absent in thermophilic and hyperthermophilic archaea. In the absence of Hsp70, how aggregating protein substrates are transferred to Hsp60 for refolding remains elusive. Here, we investigated the crosstalk in the heat shock response pathway of thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. In the present study, we biophysically and biochemically characterized one of the small heat shock proteins, Hsp14, of S. acidocaldarius. Moreover, we investigated its ability to interact with Hsp20 and Hsp60 to facilitate the substrate proteins' folding under stress conditions. Like Hsp20, we demonstrated that the dimer is the active form of Hsp14, and it forms an oligomeric storage form at a higher temperature. More importantly, the dynamics of the Hsp14 oligomer are maintained by rapid subunit exchange between the dimeric states, and the rate of subunit exchange increases with increasing temperature. We also tested the ability of Hsp14 to form hetero-oligomers via subunit exchange with Hsp20. We observed hetero-oligomer formation only at higher temperatures (50 °C-70 °C). Furthermore, experiments were performed to investigate the interaction between small heat shock proteins and Hsp60. We demonstrated an enthalpy-driven direct physical interaction between Hsp14 and Hsp60. Our results revealed that Hsp14 could transfer sHsp-captured substrate proteins to Hsp60, which then refolds them back to their active form.

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The oligomeric plasticity of Hsp20 of Sulfolobus acidocaldarius protects environment-induced protein aggregation and membrane destabilization

Cited by 21 publications

References 81 publications

Defining heat shock response for the thermoacidophilic model crenarchaeon Sulfolobus acidocaldarius

Defining heat shock response for the thermoacidophilic model crenarchaeon Sulfolobus acidocaldarius

The Cell Membrane of Sulfolobus spp.—Homeoviscous Adaption and Biotechnological Applications

Archaeal Hsp14 drives substrate shuttling between small heat shock proteins and thermosome: insights into a novel substrate transfer pathway

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