New Antibiotics Would Impede Bacterial Cytokinesis

The Z ring is composed of FtsZ protein filaments. The Z ring always forms in the middle of rod-shaped bacteria, the location being controlled by the activity of MinC. The aim of the current paper was to understand the interaction between MinC and the Z ring's FtsZ filaments.

Investigators at Johns Hopkins University (Baltimore, MD, USA) found that MinC interfered with the 3-dimensional topology formed by the FtsZ filaments during construction of the Z-ring. They reported in the February 26, 2008, online edition of the journal Current Biology that Min C controlled the scaffolding function of FtsZ by destabilized the mechanical integrity of FtsZ structures. Specifically, MinC counteracted the ability of FtsZ filaments to be in a solid-like gel state.

"The potential medical applications of our discovery are significant,” said first author Dr. Alex Dajkovic, formally a postdoctoral fellow at Johns Hopkins University, and now a researcher at Institut Curie (Paris, France). "Because the molecules involved in cell division are very similar in almost all bacteria, the process we uncovered provides a new target for the people who make antibiotics. This is extremely important because antibiotic resistance is on the rise, and many preventable deaths, especially in the developing world, are caused by bacterial infections.”


Related Links:
Johns Hopkins University
Institut Curie