Protein phosphorylation in Escherichia coli L. form NC-7

P. Freestone, S. Grant, M. Trinei, T. Onoda, V. Norris

Research output: Contribution to journalArticlepeer-review


Wall-less L-forms of Escherichia coli constitute an interesting, and relatively underused, model system for numerous studies of bacterial physiology including the cell cycle, intracellular structure and protein phosphorylation. Total extracts of the L-form revealed a pattern of protein phosphorylation similar to that of an enteropathogenic strain but very different from its parental K-12 strain. In particular, the L-form extract revealed phosphorylation on tyrosine of a protein important in pathogenesis, TypA, and calcium-specific phosphorylation of a 40 kDa protein. Two new phosphoproteins were identified in the L-form as the DNA-binding protein Dps, and YfiD, a protein of 14 kDa with homology to pyruvate formate-lyase and a region containing a tRNA cluster in bacteriophage T5.

Original languageEnglish
Pages (from-to)3289-3295
Number of pages7
Issue number12
Publication statusPublished - 1998


  • Calcium
  • Dps
  • TypA
  • Tyrosine phosphorylation
  • YfiD

ASJC Scopus subject areas

  • Microbiology


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