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Biocompatible click chemistry enabled compartment-specific pH measurement inside E-coli

Academic Article
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Overview

authors

  • Yang, M.
  • Jalloh, A. S.
  • Wei, W.
  • Zhao, J.
  • Wu, Peng
  • Chen, P. R.

publication date

  • September 2014

journal

  • Nature Communications  Journal

abstract

  • Bioorthogonal reactions, especially the Cu(I)-catalysed azide-alkyne cycloaddition, have revolutionized our ability to label and manipulate biomolecules under living conditions. The cytotoxicity of Cu(I) ions, however, has hindered the application of this reaction in the internal space of living cells. By systematically surveying a panel of Cu(I)-stabilizing ligands in promoting protein labelling within the cytoplasm of Escherichia coli, we identify a highly efficient and biocompatible catalyst for intracellular modification of proteins by azide-alkyne cycloaddition. This reaction permits us to conjugate an environment-sensitive fluorophore site specifically onto HdeA, an acid-stress chaperone that adopts pH-dependent conformational changes, in both the periplasm and cytoplasm of E. coli. The resulting protein-fluorophore hybrid pH indicators enable compartment-specific pH measurement to determine the pH gradient across the E. coli cytoplasmic membrane. This construct also allows the measurement of E. coli transmembrane potential, and the determination of the proton motive force across its inner membrane under normal and acid-stress conditions.

subject areas

  • Biocompatible Materials
  • Click Chemistry
  • Copper
  • Cytoplasm
  • Electrochemistry
  • Escherichia coli
  • Escherichia coli Proteins
  • Flow Cytometry
  • Fluorescent Dyes
  • Green Fluorescent Proteins
  • Hydrogen-Ion Concentration
  • Ions
  • Ligands
  • Membrane Potentials
  • Periplasm
  • Plasmids
  • Proton-Motive Force
  • Reactive Oxygen Species
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Identity

PubMed Central ID

  • PMC4174402

International Standard Serial Number (ISSN)

  • 2041-1723

Digital Object Identifier (DOI)

  • 10.1038/ncomms5981

PubMed ID

  • 25236616
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Additional Document Info

start page

  • 4981

volume

  • 5

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