PMID:9884220

Citation	Freestone, P, Grant, S, Trinei, M, Onoda, T and Norris, V (1998) Protein phosphorylation in Escherichia coli L. form NC-7. Microbiology (Reading, Engl.) 144 ( Pt 12):3289-95
Abstract	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.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins/metabolism; Calcium/metabolism; DNA-Binding Proteins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; GTP Phosphohydrolases; Molecular Sequence Data; Molecular Weight; Phosphoproteins/metabolism; Phosphorylation; Sequence Homology, Amino Acid; Tyrosine/metabolism
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