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Mycobacterium tuberculosis Extracellular Vesicle Enrichment through Size Exclusion Chromatography
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Rv1027c-Rv1028c encode functional KdpDE two--component system in Mycobacterium tuberculosis.

Ruchi Agrawal1, Deepak Kumar Saini1

  • 1Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560012, India.

Biochemical and Biophysical Research Communications
|March 27, 2014
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The Mycobacterium tuberculosis KdpDE two-component system is functional, with KdpD sensor kinase phosphorylating KdpE response regulator. This conserved system

Keywords:
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Area of Science:

  • Bacterial physiology and molecular mechanisms.
  • Two-component signal transduction systems in prokaryotes.

Background:

  • The Rv1027c-Rv1028c genes in Mycobacterium tuberculosis are predicted to encode the KdpDE two-component system.
  • Two-component systems are crucial for bacterial adaptation and survival, highly conserved across species.

Purpose of the Study:

  • To investigate the functional activity of the KdpDE two-component system in Mycobacterium tuberculosis.
  • To elucidate the phosphorylation mechanism and protein interactions within the KdpDE system.

Main Methods:

  • Autophosphorylation assays of KdpD sensor kinase.
  • Phosphoryl transfer studies from KdpD to KdpE response regulator.
  • Surface Plasmon Resonance (SPR) analysis to confirm protein interaction.
  • Site-directed mutagenesis to identify phosphorylation sites (His642 in KdpD, Asp52 in KdpE).
  • Protein purification with and without divalent ions, followed by refolding and chelation experiments.

Main Results:

  • The KdpDE system in M. tuberculosis is functionally active.
  • KdpD undergoes autophosphorylation and transfers the phosphoryl group to KdpE.
  • Conserved phosphorylation sites were identified at His642 (KdpD) and Asp52 (KdpE).
  • SPR confirmed a direct physical interaction between KdpD and KdpE.
  • Divalent ions are essential for KdpD phosphorylation activity.
  • KdpD and KdpE are co-transcribed as a single operon.

Conclusions:

  • The M. tuberculosis KdpDE system operates as a canonical bacterial two-component system.
  • Understanding this system provides insights into bacterial signal transduction and potential therapeutic targets.