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Microbiology 144 (1998), 3289-3295; DOI  10.1099/00221287-144-12-3289
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Protein phosphorylation in Escherichia coli L. form NC-7

P. Freestone1, S. Grant1, M. Trinei1, T. Onoda2 and V. Norris3

1 Department of Microbiology and Immunology, Medical Sciences Building, University of Leicester, Leicester LE1 9HN, UK
2 Department of Biology, Faculty of Science, Shimane University, Matsue 690, Japan
3 IFR ‘Systèmes Intégrés’, Laboratoire de Microbiologie, Faculté des Sciences et Techniques de Rouen, F76821 Mont Saint Aignan, France

ABSTRACT

Summary: 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.

Author for correspondence: V. Norris. Tel: +33 2 3514 6908. Fax: +33 2 3514 7020. e-mail: vjn@univ-rouen.fr

Keywords: Dps, YfiD, TypA, tyrosine phosphorylation, calcium




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