Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors

Gudrun S. Lukat, William R. Mccleary, Ann M. Stock, Jeffry B. Stock

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433 Scopus citations


Bacterial motility and gene expression are controlled by a family of phosphorylated response regulators whose activities are modulated by an associated family of protein-histidine kinases. In chemotaxis there are two response regulators, CheY and CheB, that receive phosphoryl groups from the histidine kinase, CheA. Here we show that the response regulators catalyze their own phosphorylation in that both CheY and CheB can be phosphorylated in the complete absence of any auxiliary protein. Both CheY and CheB use the N-phosphoryl group in phosphoramidate (NH2PO32-) as a phospho-donor. This enzymatic activity probably reflects the general ability of response regulators to accept phosphoryl groups from phosphohistidines in their associated kinases. It provides a general method for the study of activated response regulators in the absence of kinase proteins. CheY can also use intermediary metabolites such as acetyl phosphate and carbamoyl phosphate as phospho-donors. These reactions may provide a mechanism to modulate cell behavior in response to altered metabolic states.

Original languageEnglish (US)
Pages (from-to)718-722
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number2
StatePublished - 1992

All Science Journal Classification (ASJC) codes

  • General


  • Acetyl phosphate
  • Carbamoyl phosphate
  • CheB
  • CheY
  • Phosphoramidate


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