Side effects of chaperone gene co-expression in recombinant protein production
1 Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
2 Department of Genetics and Microbiology, Universitat Autònoma de Barcelona,08193, Bellaterra Barcelona, Spain
3 CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Bellaterra, 08193 Barcelona, Spain
4 Helmholtz Centre for Infection Research, Inhoffenstr. 7, 38124 Braunschweig, Germany
5 Leibniz University Hannover, Life Science - Technical Chemistry, Callinstr. 5, 30167 Hannover, Germany
Microbial Cell Factories 2010, 9:64 doi:10.1186/1475-2859-9-64Published: 2 September 2010
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.