Conversion of a soluble protein into a potent chaperone in vivo
| Autor: | Kyun-Hwan Kim, Baik Lin Seong, Kisun Ryu, Hotcherl Jeong, Ahyun Son, Seong Il Choi, Soon Bin Kwon, Keo Heun Lim |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Protein Folding medicine.medical_treatment lcsh:Medicine medicine.disease_cause Article Protein Refolding law.invention Protein Aggregates 03 medical and health sciences 0302 clinical medicine In vivo law Escherichia coli medicine lcsh:Science Binding Sites Protease Multidisciplinary biology Chemistry Escherichia coli Proteins lcsh:R Publisher Correction Recombinant Proteins In vitro Cell biology Proteostasis 030104 developmental biology Solubility Chaperone (protein) Excluded volume biology.protein Biophysics Recombinant DNA lcsh:Q Protein folding 030217 neurology & neurosurgery Molecular Chaperones Protein Binding Macromolecule |
| Zdroj: | Scientific Reports, Vol 9, Iss 1, Pp 1-13 (2019) Scientific Reports |
| DOI: | 10.1101/284802 |
| Popis: | Protein-folding assistance and aggregation inhibition by cellular factors are largely understood in the context of molecular chaperones. As an alternative and complementary model, we previously proposed that, in general, soluble cellular macromolecules including chaperones with large excluded volume and surface charges exhibit the intrinsic chaperone activity to prevent aggregation of their connected polypeptides, irrespective of the connection types, and thus to aid productive protein folding. As a proof of concept, we here demonstrated that a model soluble protein with an inactive protease domain robustly exerted chaperone activity toward various proteins harboring a short protease-recognition tag of 7 residues inEscherichia coli. The chaperone activity of this protein was similar or even superior to that of representativeE. colichaperonesin vivo. Furthermore,in vitrorefolding experiments confirmed thein vivoresults. Our findings revealed that a soluble protein exhibits the intrinsic chaperone activity, which is manifested, upon binding to aggregation-prone proteins. This study gives new insights into the ubiquitous chaperoning role of cellular macromolecules in protein-folding assistance and aggregation inhibition underlying the maintenance of protein solubility and proteostasisin vivo. |
| Databáze: | OpenAIRE |
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