Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli
The folding fate of a protein in vivo is determined by the interplay between a protein’s folding energy landscape and the actions of the proteostasis network, including molecular chaperones and degradation enzymes. The mechanisms of individual components of the E. coli proteostasis network have been...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2015-04-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124715002715 |
| _version_ | 1818269678600978432 |
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| author | Younhee Cho Xin Zhang Kristine Faye R. Pobre Yu Liu David L. Powers Jeffery W. Kelly Lila M. Gierasch Evan T. Powers |
| author_facet | Younhee Cho Xin Zhang Kristine Faye R. Pobre Yu Liu David L. Powers Jeffery W. Kelly Lila M. Gierasch Evan T. Powers |
| author_sort | Younhee Cho |
| collection | DOAJ |
| description | The folding fate of a protein in vivo is determined by the interplay between a protein’s folding energy landscape and the actions of the proteostasis network, including molecular chaperones and degradation enzymes. The mechanisms of individual components of the E. coli proteostasis network have been studied extensively, but much less is known about how they function as a system. We used an integrated experimental and computational approach to quantitatively analyze the folding outcomes (native folding versus aggregation versus degradation) of three test proteins biosynthesized in E. coli under a variety of conditions. Overexpression of the entire proteostasis network benefited all three test proteins, but the effect of upregulating individual chaperones or the major degradation enzyme, Lon, varied for proteins with different biophysical properties. In sum, the impact of the E. coli proteostasis network is a consequence of concerted action by the Hsp70 system (DnaK/DnaJ/GrpE), the Hsp60 system (GroEL/GroES), and Lon. |
| first_indexed | 2024-12-12T20:58:12Z |
| format | Article |
| id | doaj.art-91b493a5c85e427482a2079d643a323c |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-12T20:58:12Z |
| publishDate | 2015-04-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-91b493a5c85e427482a2079d643a323c2022-12-22T00:12:14ZengElsevierCell Reports2211-12472015-04-0111232133310.1016/j.celrep.2015.03.018Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coliYounhee Cho0Xin Zhang1Kristine Faye R. Pobre2Yu Liu3David L. Powers4Jeffery W. Kelly5Lila M. Gierasch6Evan T. Powers7Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USADepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USADepartments of Chemistry and Biochemistry and Molecular Biology, University of Massachusetts-Amherst, Amherst, MA 01003, USADepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USADepartment of Mathematics and Computer Science, Clarkson University, Potsdam, NY 13699, USADepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USADepartments of Chemistry and Biochemistry and Molecular Biology, University of Massachusetts-Amherst, Amherst, MA 01003, USADepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USAThe folding fate of a protein in vivo is determined by the interplay between a protein’s folding energy landscape and the actions of the proteostasis network, including molecular chaperones and degradation enzymes. The mechanisms of individual components of the E. coli proteostasis network have been studied extensively, but much less is known about how they function as a system. We used an integrated experimental and computational approach to quantitatively analyze the folding outcomes (native folding versus aggregation versus degradation) of three test proteins biosynthesized in E. coli under a variety of conditions. Overexpression of the entire proteostasis network benefited all three test proteins, but the effect of upregulating individual chaperones or the major degradation enzyme, Lon, varied for proteins with different biophysical properties. In sum, the impact of the E. coli proteostasis network is a consequence of concerted action by the Hsp70 system (DnaK/DnaJ/GrpE), the Hsp60 system (GroEL/GroES), and Lon.http://www.sciencedirect.com/science/article/pii/S2211124715002715 |
| spellingShingle | Younhee Cho Xin Zhang Kristine Faye R. Pobre Yu Liu David L. Powers Jeffery W. Kelly Lila M. Gierasch Evan T. Powers Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli Cell Reports |
| title | Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli |
| title_full | Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli |
| title_fullStr | Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli |
| title_full_unstemmed | Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli |
| title_short | Individual and Collective Contributions of Chaperoning and Degradation to Protein Homeostasis in E. coli |
| title_sort | individual and collective contributions of chaperoning and degradation to protein homeostasis in e coli |
| url | http://www.sciencedirect.com/science/article/pii/S2211124715002715 |
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