Zusammenfassung: | |
Insufficient availability of molecular chaperones is observed as a major bottleneck for proper protein folding in recombinant protein production. Therefore, co-production of selected sets of cell chaperones along with foreign polypeptides is a common approach to increase the yield of properly folded, recombinant proteins in bacterial cell factories. However, unbalanced amounts of folding modulators handling folding-reluctant protein species might instead trigger undesired proteolytic activities, detrimental regarding recombinant protein stability, quality and yield. This minireview summarizes the most recent observations of chaperone-linked negative side effects, mostly focusing on DnaK and GroEL sets, when using these proteins as folding assistant agents. These events are discussed in the context of the complexity of the cell quality network and the consequent intricacy of the physiological responses triggered by protein misfolding.
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Lizenzbestimmungen: | CC BY 2.0 Unported - https://creativecommons.org/licenses/by/2.0/ |
Publikationstyp: | Article |
Publikationsstatus: | publishedVersion |
Erstveröffentlichung: | 2010 |
Schlagwörter (englisch): | chaperone, chaperonin, Escherichia coli protein, protein ClpB, protein DnaJ, protein DnaK, recombinant protein, bacterial protein, chaperone, chaperonin, dnaK protein, E coli, Escherichia coli protein, heat shock protein 70, article, bacterial cell, cell inclusion, cell transformation, conformational transition, gene expression, growth inhibition, nonhuman, physiological process, process development, process optimization, protein aggregation, protein analysis, protein binding, protein conformation, protein degradation, protein engineering, protein folding, protein function, protein protein interaction, protein quality, protein secretion, protein synthesis, protein targeting, quality control, solubility, biosynthesis, chemistry, genetics, metabolism, protein stability, review, Bacteria (microorganisms), Bacterial Proteins, Chaperonin 60, Escherichia coli Proteins, HSP70 Heat-Shock Proteins, Molecular Chaperones, Protein Folding, Protein Stability, Recombinant Proteins |
Fachliche Zuordnung (DDC): | 500 | Naturwissenschaften, 570 | Biowissenschaften, Biologie |
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