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Study sheds new light on how cellular transport systems harness energy to perform their work inside the cell

Posted on July 9, 2013
This is a visual representation of structural alterations in the protein-conducting channel of the TIM23 complex that occur in response to changes in the energized state of the mitochondrial inner membrane. Credit: Nathan Alder

This is a visual representation of structural alterations in the protein-conducting channel of the TIM23 complex that occur in response to changes in the energized state of the mitochondrial inner membrane. Credit: Nathan Alder

Using highly sensitive fluorescent probes, a team of scientists from the University of Connecticut has captured the never-before-seen structural dynamics of an important protein channel inside the cell’s primary power plant – the mitochondrion.

The UConn team’s study found that the channel complex – known as the translocase of the inner mitochondrial membrane 23 or TIM23 – is not only directly coupled to the energized state of the mitochondrial inner membrane as scientists have long suspected, it also changes its fundamental structure - altering the helical shape of protein segments that line the channel – when voltage along the membrane’s electrical field drops.

The research, which appears this week in the peer-reviewed journal Nature Structural & Molecular Biology, explains how the energized state of the membrane drives the structural dynamics of membrane proteins and sheds new light on how cellular transport systems harness energy to perform their work inside the cell.

It also shows how fluorescent mapping at the subcelllar level may reveal new insights into the underlying causes of neurodegenerative and metabolic disorders associated with mitochondrial function.

In an overview of the research accompanying the paper’s publication, Nikolaus Pfanner of the University of Freiberg in Germany and an international leader in the field of cellular protein trafficking, and several members of his research group, called the study “a major step towards a molecular understanding of a voltage-gated protein translocase.”

Read more at: Phys.org

   
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