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Related Experiment Videos

Separate ion pathways in a Cl-/H+ exchanger.

Alessio Accardi1, Michael Walden, Wang Nguitragool

  • 1Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, MA 02454, USA.

The Journal of General Physiology
|December 1, 2005
PubMed
Summary
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Researchers identified a key glutamate residue (E203) in the CLC-ec1 transporter essential for coupling proton (H+) transport to chloride (Cl-) exchange. This finding reveals distinct pathways for Cl- and H+ within the transporter.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • CLC-ec1 is a prokaryotic transporter facilitating chloride (Cl-) and proton (H+) exchange.
  • The mechanism of H+ coupling to Cl- transport remains largely unelucidated.
  • A previously identified glutamate (E148) is crucial for extracellular proton transfer.

Purpose of the Study:

  • To investigate the role of intracellular residues in mediating H+ coupling in CLC-ec1.
  • To identify residues responsible for proton transfer from the intracellular side.
  • To elucidate the mechanism of H+ and Cl- transport pathways.

Main Methods:

  • Site-directed mutagenesis of inward-facing carboxyl-bearing residues.
  • Analysis of Cl- transport rates at different pH levels.

Related Experiment Videos

  • X-ray crystallography of mutant proteins.

    • Main Results:

    • Mutagenesis identified glutamate at position 203 (E203) as essential for H+ coupling.
    • Neutralization of E203 abolished H+ coupling, while E148A mutation allowed pH-independent transport.
    • The double mutant E148A/E203Q exhibited maximal Cl- transport, unaffected by pH.
    • X-ray structure of E203Q mutant showed similarity to wild-type CLC-ec1.

    Conclusions:

    • CLC-ec1 utilizes two distinct, partially overlapping pathways for Cl- and H+ transport.
    • These pathways converge at E148 on the extracellular side and diverge towards the intracellular side.
    • The transport mechanism deviates from traditional alternating-access models, suggesting a novel transport process.