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Ion Channels01:19

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The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
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Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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Spontaneous mutations arise infrequently during DNA replication due to errors in the process. A key factor behind these errors is tautomeric shifts in nitrogenous bases, where bases transition from keto to enol forms or amino to imino forms. This shift can alter base-pairing rules, leading to mutations. Additionally, reactive oxygen species (ROS) arising from aerobic metabolism can damage DNA, resulting in depurination (loss of a purine base) or depyrimidination (loss of a pyrimidine base).
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Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
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Atomic mutagenesis in ion channels with engineered stoichiometry.

John D Lueck1, Adam L Mackey1, Daniel T Infield1

  • 1Department of Molecular Physiology and Biophysics, The University of Iowa, Iowa City, United States.

Elife
|October 7, 2016
PubMed
Summary

C-type inactivation in potassium channels relies on a hydrogen bond network. Modifying this bond causes a key residue to flip out, allowing water entry and altering channel function.

Keywords:
C-type inactivationatomic mutagenesisbiochemistrybiophysicsintein protein ligationmolecular dynamicsnoncanonical amino acidsstructural biologyvoltage-gated sodium channelsxenopus

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Neuroscience

Background:

  • Potassium channels regulate electrical signaling in excitable cells.
  • C-type inactivation involves a hydrogen bond network in the selectivity filter.
  • Previous studies highlighted the Trp434-Asp447 hydrogen bond in Shaker potassium channels.

Purpose of the Study:

  • Investigate the role of the Trp434-Asp447 hydrogen bond in Shaker potassium channel inactivation.
  • Explore the structural and electrostatic consequences of modifying this hydrogen bond.
  • Develop a novel protein engineering system for stoichiometric control of channel subunits.

Main Methods:

  • Molecular dynamics simulations to model channel behavior.
  • Protein engineering using split inteins and ERret motifs.
  • Nonsense suppression techniques (previously).

Main Results:

  • Mutation of Trp434 to Ind caused Asp447 to flip extracellularly.
  • This flip allowed water penetration and reduced local negative charge.
  • The split intein system achieved stoichiometric control of Shaker monomers and multi-amino acid encoding.

Conclusions:

  • The Trp434-Asp447 hydrogen bond is crucial for maintaining the integrity of the Shaker potassium channel selectivity filter.
  • Structural rearrangements upon mutation impact water permeation and electrostatics.
  • The developed protein engineering system offers precise control over ion channel assembly.