The histidine kinase CusS senses silver ions through direct binding by its sensor domain

Swapna A. Gudipaty, Megan M. McEvoy

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


The Cus system of Escherichia coli aids in protection of cells from high concentrations of Ag(I) and Cu(I). The histidine kinase CusS of the CusRS two-component system functions as a Ag(I)/Cu(I)-responsive sensor kinase and is essential for induction of the genes encoding the CusCFBA efflux pump. In this study, we have examined the molecular features of the sensor domain of CusS in order to understand how a metal-responsive histidine kinase senses specific metal ions. We find that the predicted periplasmic sensor domain of CusS directly interacts with Ag(I) ions and undergoes a conformational change upon metal binding. Metal binding also enhances the tendency of the domain to dimerize. These findings suggest a model for activation of the histidine kinase through metal binding events in the periplasmic sensor domain.

Original languageEnglish (US)
Pages (from-to)1656-1661
Number of pages6
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number9
StatePublished - Sep 2014


  • Copper
  • Cus system
  • CusS
  • Histidine kinase
  • Silver
  • Two-component system

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology


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