Escherichia coli protein degradation

Goldberg AL (1972) Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin). Proc Natl Acad Sci USA 69 422 26... 

Busse H-J, Wostmann C, Bakker EP The bactericidal action of streptomycin Membrane permeabilization caused by the insertion of mistranslated proteins into the cytoplasmic membrane of Escherichia coli and subsequent caging of the antibiotic inside the cells due to degradation of these proteins. J Gen Microbiol 1992 138 551. [PMID 1375623]... 

Protein expression and purification have traditionally been time-consuming, case-specific endeavors, and are considered to be the greatest bottlenecks in most proteomics pipelines (1) Escherichia coli (E. coli) is the most convenient and cost-effective host, although optimal conditions for the expression of different proteins vary widely. Proteins vary in their structural stability, solubility, and toxicity in this environment, resulting in differing rates of protein degradation,... 

Golf, S. A. and Goldberg, A. L. (1987) An increased content of protease La, the Ion gene product, increases protein degradation and blocks growth in Escherichia coli. J. Biol. Chem. 262, 4508-4515. 

A. Kuroda, S. Tanaka, T. Ikeda, J. Kato, N. Takiguchi and H. Ohtake (1999). Inorganic polyphosphate kinase is required to stimulate protein degradation and for adaptation to amino acid starvation in Escherichia coli. Proc. Natl. Acad. Sci. USA, 96, 14264-14269. 

Escherichia coli Easy to grow in large-scale volumes Transcriptional and translational control well known Successfully used in the manufacture of insulin, interferon and human somatotropin Difficult to achieve export of some proteins into growth medium Degradation of small proteins by proteases Unable to undertake most post-translational modifications, e.g. glycosylation Many proteins retained in the cytoplasm as insoluble aggregates... 

Thompson, M. W., Singh, S. K., and Maurizi, M. R. (1994). Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis. J. Biol. Chem. 269, 18209-18215. 

Lange, A.J. Li, L. Vargas, A.M. Pilkis, S.J. Expression of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli. Role of N-2 proline in degradation of the protein. J. Biol. Chem., 268, 8078-8084 (1993)... 

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