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Microbiology 144 (1998), 3289-3295
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microbiology, Vol 144, 3289-3295, Copyright © 1998 by Society for General Microbiology

ARTICLES

Protein phosphorylation in Escherichia coli L. form NC-7

P Freestone, S Grant, M Trinei, T Onoda and V Norris
Department of Microbiology and Immunology, University of Leicester, UK.

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.


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