ArticleScientific reports2016
Suppression of amyloid fibrils using the GroEL apical domain.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Single-molecule characterization of salivary protein aggregates from Parkinson's disease patients: a pilot study.Brain communications · 2024Article
- GroEL-A Versatile Chaperone for Engineering and a Plethora of Applications.Biomolecules · 2022Review
- Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases.International journal of molecular sciences · 2022Review
- Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein ofInternational journal of molecular sciences · 2021Article
- Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein.International journal of molecular sciences · 2019Article
- Acid-denatured small heat shock protein HdeA fromThe Journal of biological chemistry · 2019Article
- Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle.Science advances · 2018Article
- The versatile mutational "repertoire" of Escherichia coli GroEL, a multidomain chaperonin nanomachine.Biophysical reviews · 2018Review
- The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms.Frontiers in molecular biosciences · 2018Article
- How accurate are your simulations? Effects of confined aqueous volume and AMBER FF99SB and CHARMM22/CMAP force field parameters on structural ensembles of intrinsically disordered proteins: Amyloid-βIntrinsically disordered proteins · 2017Article
- Modulating the Effects of the Bacterial Chaperonin GroEL on Fibrillogenic Polypeptides through Modification of Domain Hinge Architecture.The Journal of biological chemistry · 2016Article
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Authors and funding
5 authors.
Funding
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Abstract
In E. coli cells, rescue of non-native proteins and promotion of native state structure is assisted by the chaperonin GroEL. An important key to this activity lies in the structure of the apical domain of GroEL (GroEL-AD) (residue 191-376), which recognizes and binds non-native protein molecules through hydrophobic interactions. In this study, we investigated the effects of GroEL-AD on the aggregation of various client proteins (α-Synuclein, Aβ42, and GroES) that lead to the formation of distinct protein fibrils in vitro. We found that GroEL-AD effectively inhibited the fibril formation of these three proteins when added at concentrations above a critical threshold; the specific ratio differed for each client protein, reflecting the relative affinities. The effect of GroEL-AD in all three cases was to decrease the concentration of aggregate-forming unfolded client protein or its early intermediates in solution, thereby preventing aggregation and fibrillation. Binding affinity assays revealed some differences in the binding mechanisms of GroEL-AD toward each client. Our findings suggest a possible applicability of this minimal functioning derivative of the chaperonins (the "minichaperones") as protein fibrillation modulators and detectors.
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