A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins

Fatima, Komal; Naqvi, Fatima; Younas, Hooria

doi:10.1007/s12013-021-00970-5

Cited by 26 publications

(23 citation statements)

References 171 publications

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“…This is often summarized as the proteostasis network. The most obvious part of the proteostasis network relevant to combat protein aggregation, are the chaperones that assist proteins in adopting their nonamyloid native and functional conformation. − Also, degradation of proteins via the proteasome pathway , or via autophagy is relevant in that regard …”

Section: Amyloids and Evolution Of Defense Strategiesmentioning

confidence: 99%

Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids

et al. 2021

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This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are an important hallmark of protein misfolding diseases and therefore have been investigated for decades. Only recently, however, atomic or near-atomic resolution structures have been elucidated from various in vitro and ex vivo obtained fibrils. In parallel, the process of fibril formation has been studied in vitro under highly artificial but comparatively reproducible conditions. The review starts with a summary of what is known and speculated from artificial in vitro amyloid-type protein aggregation experiments. A partially hypothetic fibril selection model will be described that may be suitable to explain why amyloid fibrils look the way they do, in particular, why at least all so far reported high resolution cryo-electron microscopy obtained fibril structures are in register, parallel, cross-β-sheet fibrils that mostly consist of two protofilaments twisted around each other. An intrinsic feature of the model is the prion-like nature of all amyloid assemblies. Transferring the model from the in vitro point of view to the in vivo situation is not straightforward, highly hypothetic, and leaves many open questions that need to be addressed in the future.

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Section: Amyloids and Evolution Of Defense Strategiesmentioning

confidence: 99%

Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids

et al. 2021

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“…They optimize the physiological responses of bacteria by interacting directly with other proteins, taking part in cell signaling, and acting as stress response proteins ( Hartl and Hayer-Hartl, 2002 ). Chaperones GroEL and DnaK are the main representatives of their families ( Cooper and Hausman, 2000 ; Beckerman, 2005 ; Liberek et al, 2008 ), and their action has been described in a wide range of bacteria, frequently working together ( Fourie and Wilson, 2020 ; Fatima et al, 2021 ; Mayer, 2021 ) and taking part in the regulation of transcription and translation ( Parsot et al, 2003 ).…”

Section: Discussionmentioning

confidence: 99%

Comparative Proteomic Analysis of Psychrophilic vs. Mesophilic Bacterial Species Reveals Different Strategies to Achieve Temperature Adaptation

2022

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The old debate of nature (genes) vs. nurture (environmental variables) is once again topical concerning the effect of climate change on environmental microorganisms. Specifically, the Polar Regions are experiencing a drastic increase in temperature caused by the rise in greenhouse gas emissions. This study, in an attempt to mimic the molecular adaptation of polar microorganisms, combines proteomic approaches with a classical microbiological analysis in three bacterial species Shewanella oneidensis, Shewanella frigidimarina, and Psychrobacter frigidicola. Both shewanellas are members of the same genus but they live in different environments. On the other hand, Shewanella frigidimarina and Psychrobacter frigidicola share the same natural environment but belong to a different genus. The comparison of the strategies employed by each bacterial species estimates the contribution of genome vs. environmental variables in the adaptation to temperature. The results show a greater versatility of acclimatization for the genus Shewanella with respect to Psychrobacter. Besides, S. frigidimarina was the best-adapted species to thermal variations in the temperature range 4–30°C and displayed several adaptation mechanisms common with the other two species. Regarding the molecular machinery used by these bacteria to face the consequences of temperature changes, chaperones have a pivoting role. They form complexes with other proteins in the response to the environment, establishing cooperation with transmembrane proteins, elongation factors, and proteins for protection against oxidative damage.

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“…The second possible explanation that might explain the detected correlations includes the effects of psychological stress on the expression of molecular chaperones. Chaperons are proteins with a major role in the regulation of protein conformational folding (Roufayel & Kadry, 2019; Fatima et al, 2021). Folding of histone proteins in nuclear chromatin, and formation of nucleosomes from histones and DNA is also an important function of chaperons.…”

Section: Discussionmentioning

confidence: 99%