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Related Experiment Videos

A sensor for intracellular ionic strength.

Esther Biemans-Oldehinkel1, Nik A B N Mahmood, Bert Poolman

  • 1Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.

Proceedings of the National Academy of Sciences of the United States of America
|July 4, 2006
PubMed
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Cystathionine-beta-synthase (CBS) domains in the OpuA transporter sense ionic strength to regulate activity. This electrostatic switching mechanism controls membrane transport based on cellular ionic conditions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Cystathionine-beta-synthase (CBS) domains are widespread but their functions remain largely uncharacterized.
  • Tandem CBS domains are frequently found in membrane transport proteins, including the ATP-binding cassette (ABC) superfamily.

Purpose of the Study:

  • To elucidate the function of tandem CBS domains in the osmoregulatory ABC transporter OpuA.
  • To investigate the role of CBS domains in sensing and responding to ionic strength.

Main Methods:

  • Biochemical assays to measure transporter activity.
  • Site-directed mutagenesis to modify CBS domains.
  • Analysis of ionic strength dependence of OpuA transport.

Main Results:

Related Experiment Videos

  • Tandem CBS domains in OpuA function as sensors for ionic strength.
  • Transport activity is regulated by an electrostatic switching mechanism controlled by ionic strength and membrane surface charge.
  • Modifications to CBS domains alter the transporter's sensitivity to ionic strength.

Conclusions:

  • CBS domains play a critical role in sensing ionic strength to control membrane transport.
  • A model for ionic strength-gated membrane transport mediated by CBS domains is proposed.
  • This study reveals a novel function for CBS domains in cellular osmoregulation.