"ATP is the energy currency of life," Chapter said. In the reaction of the biological system, the ATP phosphodiester bond requires a certain amount of energy to drive. The combination of DX protein consumes the energy of ATP in the cell, disrupts the normal metabolic activity of the cell, and prevents cell division, but the cells are still continuing to grow. After being exposed to the DX protein, E. coli develops from a normal sphere to a slender filament. In filamentous bacteria, dense intracellular lipid structures are divided to form cells of the same length. The researchers call this unusual structure that has not been seen before as internal liposomes.
"These dense lipid structures are forming very regular areas. They are gradually forming along the filamentous cells. They look like a defense mechanism that makes the cells divide themselves." Chapult said. This unique adaptation process has never been observed in bacterial cells, and it is the only one that appears in single-cell organisms. Synthesizing protein DX is not an easy task. It needs to carefully mimic the characteristics of protein folding in its natural state and can be combined with the key metabolite ATP.
Scientists will next study how these cells respond when they encounter new conditions. For example, how do cells respond to an unfamiliar synthetic protein? The study also pointed out that many infectious pathogens rely on being dormant (similar to the viable but non-cultivable state observed in DX exposed E. coli) to avoid antibiotic testing. This discovery provides a better method for studying the behavior of these pathogens. In addition, the inhibition of ATP, which is extremely important for organisms, can provide another way to prevent and treat diseases.
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