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Volume 144, Issue 12

Protein phosphorylation in L. form NC-7 Free

Abstract

Summary: Wall-less L-forms of 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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Keyword(s): calcium , Dps , TypA , tyrosine phosphorylation and YfiD
© Society for General Microbiology 1998
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1998-12-01
2024-04-20
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Protein phosphorylation in Escherichia coli L. form NC-7
Microbiology 144, 3289 (1998); https://doi.org/10.1099/00221287-144-12-3289
/content/journal/micro/10.1099/00221287-144-12-3289
/content/journal/micro/10.1099/00221287-144-12-3289
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