Review: Mechanisms of Disaggregation and Refolding of Stable Protein Aggregates by Molecular Chaperones

Ben‐Zvi, Anat; Goloubinoff, Pierre

doi:10.1006/jsbi.2001.4352

Cited by 211 publications

(147 citation statements)

References 73 publications

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“…These effects are similar to those of natural molecular chaperones. 4 The SAXS data show that the size and conformation of the protein are similar during heating up to 60°C in both solutions. Above this temperature, and also during cooling, the average R g values of the system in P188 solution remain larger (by about 3 Å) when compared to that in the neat solution.…”

Section: Discussionmentioning

confidence: 89%

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Surfactant Copolymers Prevent Aggregation of Heat Denatured Lysozyme

et al. 2006

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We investigated the ability of certain triblock copolymer surfactant poloxamers of the form polyethylene oxide-polypropylene oxide-polyethylene oxide (PEO-PPO-PEO), to prevent formation of stable aggregates of heat denatured hen egg lysozyme. Differential scanning calorimetry (DSC) and synchrotron small angle x-ray scattering (SAXS) experiments were performed to study the thermodynamics and solution structures of lysozyme at temperatures between 20 and 90°C in the presence and absence of poloxamers with various molecular weights (8.4-14.3 kDa), but similar hydrophile/hydrophobe (PEO:PPO) ratio of 80%. Poloxmer 188 was found to be very effective in preventing aggregation of heat denatured lysozyme and those functioned as a synthetic surfactant, thus enabling them to refold when the conditions become optimal. For comparison, we measured the ability of 8 kDa polyethylene glycol (PEG) to prevent lysozyme aggregation under same conditions. The results of these studies suggest that poloxamers are more efficient than PEG in preventing aggregation of heat denaturated lysozyme, To achieve equivalence, more than an order of magnitude higher concentration of PEG concentration was needed. Apparently, the presence of a hydrophobic segment in the poloxamers increases their ability to target the hydrophobic region of the unfolded proteins and protect them from self association. Given their biocompatibility and the low concentrations at which they effectively facilitate refolding of denatured proteins, they may be useful in the treatment of burns and other conditions resulting in the denaturation of proteins.

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Section: Discussionmentioning

confidence: 89%

“…4 The mechanism of refolding by HSPs, usually involves binding to the unfolded proteins to prevent or reduce the self-association of denatured proteins. 13,45 In principle, unfolded proteins may spontaneously refold to their native states, or intermediate states, if their aggregation is prevented.…”

Section: Introductionmentioning

confidence: 99%

Surfactant Copolymers Prevent Aggregation of Heat Denatured Lysozyme

et al. 2006

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“…Hsp70 members are highly multifunctional proteins that have been shown to play a key role in proteome maintenance, such as in de novo protein folding (co-or post-translational), protein translocation across membranes (Lyman and Schekman, 1997;Matlack et al, 1999;Young et al, 2003), refolding of stress damaged proteins (Ben-Zvi et al, 2004;Schroder et al, 1993;Sharma et al, 2010), in preventing protein aggregation (Auluck et al, 2002;Broadley and Hartl, 2009;Klucken et al, 2004;Sakahira et al, 2002;Warrick et al, 1999), disaggregation (Ben-Zvi and Goloubinoff, 2001;Diamant et al, 2000;Liberek et al, 2008;Shorter, 2011) and degradation of irreparable misfolded proteins (Bercovich et al, 1997;Fisher et al, 1997;Urushitani et al, 2004). These essential and diverse cellular functions of Hsp70 are attributed to its physical interaction with various co-chaperones such as Hsp40, NEFs and with proteins such as HIP, HOP and CHIP.…”

Section: Ii41121 the Hsp70 Chaperone Systemmentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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“…Moreover, the osmolyte accumulation under drought can lead to misfolding and aggregation of proteins [39], and these changes can potentially limit cells' responses to desiccation [40]. Therefore, to better understand the drought resistant mechanism in E. pusillum, we investigated the expression changes of genes commonly involved in the response to stresses in other organisms, such as oxidative stress, osmotic regulation and post-translational processing under our drought treatment.…”

Section: The Expression Changes Of Gene Commonly Involved In Stress Rmentioning

confidence: 99%

Comparative transcriptome analysis of the lichen-forming fungus Endocarpon pusillum elucidates its drought adaptation mechanisms

Wang

Zhang

Zhou

et al. 2014

Sci. China Life Sci.

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The lichen-forming fungus was isolated from the desert lichen Endocarpon pusillum that is extremely drought resistant. To understand the molecular mechanisms of drought resistance in the fungus, we employed RNA-seq and quantitative real-time PCR to compare and characterize the differentially expressed genes in pure culture at two different water levels and with that in desiccated lichen. The comparative transcriptome analysis indicated that a total of 1781 genes were differentially expressed between samples cultured under normal and PEG-induced drought stress conditions. Similar to those in drought resistance plants and non-lichenized fungi, the common drought-resistant mechanisms were differentially expressed in E. pusillum. However, the expression change of genes involved in osmotic regulation in E. pusillum is different, which might be the evidence for the feature of drought adaptation. Interestingly, different from other organisms, some genes involved in drought adaption mechanisms showed significantly different expression patterns between the presence and absence of drought stress in E. pusillum. The expression of 23 candidate stress responsive genes was further confirmed by quantitative real-time PCR using dehydrated E. pusillum lichen thalli. This study provides a valuable resource for future research on lichen-forming fungi and shall facilitate future functional studies of the specific genes related to drought resistance. lichen, mycobiont, dehydration, drought adaption, drought resistant Citation:Wang YY, Zhang XY, Zhou QM, Zhang XL, Wei JC. Comparative transcriptome analysis of the lichen-forming fungus Endocarpon pusillum elucidates its drought adaptation mechanisms.

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Review: Mechanisms of Disaggregation and Refolding of Stable Protein Aggregates by Molecular Chaperones

Cited by 211 publications

References 73 publications

Surfactant Copolymers Prevent Aggregation of Heat Denatured Lysozyme

Surfactant Copolymers Prevent Aggregation of Heat Denatured Lysozyme

Firefly luciferase mutants as sensors of proteome stress

Comparative transcriptome analysis of the lichen-forming fungus Endocarpon pusillum elucidates its drought adaptation mechanisms

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