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Discovered proteins help bacteria multiply

Researchers at Lund University in Sweden have discovered two proteins that play a role when bacteria cells divide in order to multiply. In the future the discovery will make it easier to develop much-needed new antibiotics as antibiotic resistance gets worse.
The yellow rings show where the bacteria Streptomyces venezuelae will divide.
The yellow rings show where the bacteria Streptomyces venezuelae will divide. Photo: Sebastian Wasserstrom and Yusak Budi Susilo

Together with their British colleagues from the John Innes Centre in Norwich the biologists from Lund have investigated genes from the bacteria family Streptomyces. The researchers have discovered a new function when it comes to the division of cells into new cells.

All cells, including bacteria cells, divide themselves in order to multiply and propagate. The division is carried out by a protein that forms a circular structure on the inside of the cell. The ring attracts other proteins that continue to build the wall inside the cell. In this way a transverse wall is created, and this wall finally makes the cell split into two cells.

”You can compare it to a belt inside the cell. The ringlike protein structure is the first step when a cell splits and become two cells,” says Klas Flärdh, professor at the Department of Biology in Lund.

The research teams in Lund and Norwich have reached their results through a combination of molecular analysis and advanced microscopy.

Klas Flärdh emphasizes that it is still basic research. But he also points out that more and more knowledge about bacteria cells and how they multiply will have practical use in the future. One field where this knowledge can be applied is in the development of new types of antibiotics.

”The whole machinery behind bacterial cell division is a very promising target to attack with new antibiotics. More knowledge about the molecular mechanisms behind the division of cells will be of great value,” says Klas Flärdh.

The results are presented in an article in PNAS.

Jan Olsson  

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