@phdthesis{Dolata2019,
  author    = {Katarzyna Dolata},
  title     = {Proteomics-based analysis of stress responses during recombinant protein production in Escherichia coli},
  journal    = {Proteomik-basierende Analysen der Stress-Antwort von Escherichia coli w{\"a}hrend rekombinanter Proteinproduktion},
  url       = {https://nbn-resolving.org/urn:nbn:de:gbv:9-opus-29819},
  pages     = {153},
  year      = {2019},
  abstract  = {Escherichia coli has been commonly used as a platform for recombinant protein production and accounts for approximately 30\% of current biopharmaceuticals on the market. Nowadays, many recombinant proteins require post-translational modifications which E. coli normally cannot facilitate. Therefore, novel technological advancements are unceasingly being developed to improve the E. coli expression system. In this work, some of the most recently engineered platforms for the production of disulfide bond-containing proteins were used to study the E. coli proteome under heterologous protein production stress. The effects of protein secretion via the Sec and Tat translocation pathways were examined using a comparative LC-MS/MS analysis. The E. coli proteome responds to foreign protein production by activation of several overlapping stress responses with a high degree of interaction. In consequence, a number of important cellular processes such as cellular metabolism, protein transport, redox state of the cytoplasm and membrane structure are altered by the production stress. These changes lead to the reduction of cellular growth and recombinant product yields. Resolving the identified bottlenecks will increase the efficiency of recombinant protein expression processes in E. coli.},
  language  = {en}
}