Duke scientists deconstruct process of bacterial division

DURHAM, N.C. -- Duke University researchers have made a major advance in understanding how bacteria divide. This could lead to new antibiotic treatments that prevent dangerous bacteria from multiplying.

Normally, bacteria divide by forming a ring that pinches the cell in two. The ring is called a “Z ring” after the protein FtsZ, which forms a ring-shaped scaffold and then squeezes it smaller. In bacteria, the Z ring also contains a dozen other proteins, all believed to be essential for division.

The Z ring normally pulls in on the cell membrane by binding to another protein, FtsA, which has one end attached to the inner cell membrane and the other end connected to FtsZ. When the Z ring constricts, it completely pulls in the membrane and nips the bacterium in two.

But cell biology research scientist Masaki Osawa, Ph.D., cut FtsA out of the system by making an FtsZ that could bind directly to the membrane, and called it "membrane targeted FtsZ" or FtsZ-mts.

First, Osawa demonstrated that the new protein, FtsZ-mts, assembled Z rings in bacteria.

Then he constructed a greatly simplified cell-division machine in microscopic oil droplets, called liposomes, that demonstrated the important role of FtsZ in the division process. He was able to assemble Z rings in this completely artificial system, the liposome, a tiny hollow sphere of fat that mimics natural cell membranes.

To do this, Osawa mixed the liposomes with FtsZ and GTP, a molecule that provides energy. On a microscope slide the liposomes fused and stretched into tubes that mimicked the shape of E. coli and other rod-shaped bacteria.

“It was a happy coincidence that the size and shape of the liposomes was similar to that of rod-shaped bacteria,” says co-author Harold Erickson, professor of cell biology. “These tubular liposomes are a new micro-structure, and their formation is still a mystery.”