Identification of phosphoproteins in Escherichia coli

P. Freestone, S. Grant, I. Tóth, V. Norris

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

The substrates of ion- and lipid-stimulated protein kinase activity in extracts of Escherichia coli were purified by chromatography. Subsequent N-terminal sequencing suggests that these substrates include the following: a novel 80 kDa protein co-purifying with RNA polymerase but partially homologous to elongation factor G; a protein with an apparent molecular weight of 65 kDa identified as the ribosomal protein S1; and a 32 kDa protein identified as succinyl CoA synthetase, a key enzyme in the tricarboxylic acid cycle. The phosphorylation of these three proteins was markedly stimulated by the addition of manganese, and occurred on threonine, serine or tyrosine residues as indicated by the stability of the phosphoresidues during acid treatment. In addition, a calcium-stimulated protein of 70 kDa was identified as the heat-shock protein DnaK, and a 17 kDa lipid-stimulated phosphoprotein as nucleotide diphosphate kinase.

Original languageEnglish
Pages (from-to)573-580
Number of pages8
JournalMolecular Microbiology
Volume15
Issue number3
DOIs
Publication statusPublished - Feb 1995

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Phosphoproteins
Escherichia coli
Proteins
Succinate-CoA Ligases
Peptide Elongation Factor G
Lipids
Citric Acid Cycle
Diphosphates
Threonine
DNA-Directed RNA Polymerases
Manganese
Heat-Shock Proteins
Protein Kinases
Serine
Tyrosine
Chromatography
Phosphotransferases
Nucleotides
Molecular Weight
Phosphorylation

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Identification of phosphoproteins in Escherichia coli. / Freestone, P.; Grant, S.; Tóth, I.; Norris, V.

In: Molecular Microbiology, Vol. 15, No. 3, 02.1995, p. 573-580.

Research output: Contribution to journalArticle

Freestone, P. ; Grant, S. ; Tóth, I. ; Norris, V. / Identification of phosphoproteins in Escherichia coli. In: Molecular Microbiology. 1995 ; Vol. 15, No. 3. pp. 573-580.
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