Research Highlights

New clue into bug breaking

Biplab Das

doi:10.1038/nindia.2008.317 Published online 11 November 2008

The bacterial cell divides due to a force generated in a ring like structure made of protein filaments and other cellular chemicals. A group of researchers has now put forward a model that will be useful in designing new antibiotics that could halt cell division of bacteria1. This might help design new weapons to tame unruly antibiotic-resistant bacteria.

The researchers studied the rod-shaped bacteria Escherichia coli that inhabit the human gut. They found that filamenting temperature sensitive Z (FtsZ) protein, anchor proteins (protein that links FtsZ to cell wall), and guanosine triphosphate (GTP) work in concert to generate a stress. FtsZ proteins form a ring like structure known as Z ring. When FtsZ mediated hydrolysis convert GTP to GDP (guanosine diphosphate) in the outer layer of Z ring, the outer layer tends to bend. But the intact GTP of inner layer resists immediate bending. This generates a stress, which is transmitted to the cell wall via the anchor proteins.

The stress generates a contractile force of few piconewtons (one trillionth of a Newton). This fuels inward movement of the cell wall at the mid-section of bacterial cell coupled with generation of a septum made of peptidoglycan consisting of sugars and amino acids. This divides a bacterial cell into two halves.

"This model offers a plausible explanation for the contraction of Z-ring, which seems to drive the constriction at the mid-cell," says lead researcher Anirban Sain. New routes, such as targeting the Z ring, to stop bacterial proliferation have become urgent since antibiotic resistance is on the rise, he adds.

The authors of this work are from: Physics Department, Indian Institute of Technology–Bombay, Powai, Mumbai, India, Theoretical Physics Division, Bhabha Atomic Research Center, Trombay, Mumbai, India.


References

  1. Ghosh, B. et al. Origin of Contractile Force during Cell Division of Bacteria. Phys. Rev. Lett. 101, 178101 (2008) | Article |