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Labeling DNA Probes03:31

Labeling DNA Probes

DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...

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Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
09:17

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay

Published on: January 11, 2017

Activity-based probe for histidine kinase signaling.

Kaelyn E Wilke1, Samson Francis, Erin E Carlson

  • 1Department of Chemistry, Indiana University, Bloomington, 47405, United States.

Journal of the American Chemical Society
|May 22, 2012
PubMed
Summary

Researchers developed a novel activity-based probe to detect bacterial histidine kinase (HK) activity. This probe labels active HK proteins, offering a new strategy for studying two-component systems (TCSs) and identifying potential drug targets.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Bacterial two-component systems (TCSs) regulate essential cellular functions.
  • Histidine kinases (HKs) are key signaling proteins within TCSs, initiating signal transduction via phosphorylation.
  • Current methods for profiling HK activity are insufficient, hindering research and therapeutic development.

Purpose of the Study:

  • To develop a novel method for direct readout of HK activity.
  • To overcome the challenge of detecting unstable phosphohistidine intermediates.
  • To create an activity-based probe for analyzing HK-mediated signaling.

Main Methods:

  • Design and synthesis of a fluorophore-conjugated ATP analog, BODIPY-FL-ATPγS.
  • Utilizing a γ-thiophosphorylated ATP analog to generate a more stable thiophosphorylated histidine intermediate.
  • Characterizing the probe's ability to label active HK proteins and its competition for the ATP binding site.

Main Results:

  • BODIPY-FL-ATPγS successfully labels active bacterial histidine kinases.
  • The probe competes with ATP for binding to the HK active site.
  • This indicates the probe accurately reflects HK activity.

Conclusions:

  • BODIPY-FL-ATPγS is a valuable activity-based probe for studying bacterial TCSs.
  • This probe enables direct detection of HK activity, facilitating functional studies.
  • The probe aids in the identification of inhibitors targeting HKs for therapeutic purposes.