Tyrosine phosphorylation in Escherichia coli

J Mol Biol. 1998 Jun 26;279(5):1045-51. doi: 10.1006/jmbi.1998.1836.


The phosphorylation on tyrosine of a protein in Escherichia coli both in vivo and in vitro was revealed by recognition by anti-phosphotyrosine antibodies, labelling with [gamma-32P]ATP, and phosphoamino acid analysis. This protein, which we name TypA, is the product of the o591 reading frame as revealed by N-terminal sequencing and antibody cross-reactivity. Inactivation of typA altered the patterns of protein synthesis during both exponential growth and carbon starvation. These alterations included the disappearance of an acidic isoform of both the universal stress protein UspA and carbon starvation protein Csp15, and increased synthesis of the histone-like protein H-NS. The sequence of TypA from strain K-12 differs from that of an enteropathogenic strain in six amino acid residues and the protein is three residues shorter. We propose that TypA interacts with global regulatory networks and that its phosphorylation may be relevant to pathogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / immunology
  • Bacterial Proteins / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / immunology
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • GTP Phosphohydrolases*
  • Heat-Shock Proteins / immunology
  • Heat-Shock Proteins / metabolism
  • Molecular Sequence Data
  • Phosphoproteins*
  • Phosphorylation
  • Radioactive Tracers
  • Tyrosine / immunology
  • Tyrosine / metabolism*


  • Bacterial Proteins
  • Escherichia coli Proteins
  • Heat-Shock Proteins
  • Phosphoproteins
  • Radioactive Tracers
  • universal stress protein A, Bacteria
  • Tyrosine
  • Adenosine Triphosphate
  • GTP Phosphohydrolases
  • typA protein, E coli

Associated data

  • GENBANK/AF058333