Enhanced production of recombinant proteins in Escherichia coli by filamentation suppression

Appl Environ Microbiol. 2003 Feb;69(2):1295-8. doi: 10.1128/AEM.69.2.1295-1298.2003.

Abstract

During growth of high-cell-density cultures of Escherichia coli, overproduction of recombinant proteins often results in increased stress response, cell filamentation, and growth cessation. Filamentation of cells consequently lowers final achievable cell concentration and productivity of the target protein. Reported here is a methodology that should prove useful for the enhancement of cell growth and protein productivity by the suppression of cell filamentation. By the coexpression of the E. coli ftsA and ftsZ genes, which encode key proteins in cell division, growth of recombinant strains as well as production of human leptin and human insulin-like growth factor I was improved. Observation of cell morphology revealed that the coexpression of the ftsA and ftsZ genes successfully suppressed filamentation caused by the accumulation of recombinant proteins.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Culture Media
  • Cytoskeletal Proteins*
  • Escherichia coli / cytology*
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Humans
  • Insulin-Like Growth Factor I / genetics
  • Insulin-Like Growth Factor I / metabolism
  • Leptin / genetics
  • Leptin / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*

Substances

  • Bacterial Proteins
  • Culture Media
  • Cytoskeletal Proteins
  • Escherichia coli Proteins
  • FtsA protein, Bacteria
  • FtsA protein, E coli
  • FtsZ protein, Bacteria
  • Leptin
  • Recombinant Fusion Proteins
  • Insulin-Like Growth Factor I