New Approaches to Understanding Bacterial Histidine Kinase Activity and Inhibition

Kaelyn E. Wilke, Erin E Carlson

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations

Abstract

Bacteria rely on signal transduction pathways to respond to environmental changes. Many of these pathways are two-component systems (TCSs). The prototypical TCS includes two proteins that are often encoded on the same operon and have molecular recognition for one another: a membrane-bound histidine kinase (HK) and a cytosolic response regulator (RR). Bacterial HKs are typically homodimeric, periplasmic sensing proteins anchored to the membrane. The most direct way of detecting TCS activity is by monitoring the phosphorylation of its proteins, for which radioactive adenosine triphosphate (ATP) assays have traditionally been used. The ideal use of an ABP will be the global profiling of HKs from various sample types or screening of inhibitors. HKs of TCSs are excellent drug targets as it is well established that HKs aid in bacterial survival and virulence. Preventing these signaling pathways from transmitting information would be a new way of treating bacterial infections.

Original languageEnglish (US)
Title of host publicationKinomics
Subtitle of host publicationApproaches and Applications
PublisherWiley
Pages233-254
Number of pages22
ISBN (Electronic)9783527683031
ISBN (Print)9783527337651
DOIs
StatePublished - Oct 1 2015

Keywords

  • Bacterial Histidine Kinase Activity
  • Bacterial Histidine Kinase Inhibition
  • Phosphorylation
  • Protein kinases
  • Two-Component System Signaling

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