Phosphorylation of an Escherichia coli protein at tyrosine

J Mol Biol. 1986 Jan 20;187(2):305-8. doi: 10.1016/0022-2836(86)90236-6.

Abstract

The analysis of protein phosphorylation in the bacterium Escherichia coli showed that, while most phosphoproteins are modified at serine and/or threonine residues, one of them is modified exclusively at tyrosine. This particular protein which has a molecular weight of 54,500 and a pHi value of 5.6 is found associated with the membrane/ribosome fraction of the cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Autoradiography
  • Bacterial Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / metabolism*
  • Isoelectric Focusing
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Tyrosine*

Substances

  • Bacterial Proteins
  • Phosphoproteins
  • Tyrosine