Scientists have discovered a protein that allows bacteria to close in inactive spores under extreme conditions. The process, which allows bacteria to become practically indestructible, explains why bacteria can survive in uninhabitable places such as permafrost, in the depths of the ocean or in the outer space.
This ability to sporular, known as sporulation, also allows superbacteria to evade hospital cleaning and then return to life in the bowels of committed patients.
Upon discovering a new protein involved in sporulation in a group of bacteria, scientists hope that our understanding of the ability of bacteria to survive against probabilities, and even open new paths for antimicrobial therapies can be deepened.
The study, covered in two separate articles published in and Development genes today, analyzes Bacillus, a group of bacteria, including cereus, responsible for food poisoning and anthrax. The research team included scientists from the Department of Chemistry, King’s College London, the University of California in San Diego, the Max Planck unit for the science of pathogens in Berlin and Mount Holyake College in the United States.
Professor Rivka Isaacson, co -author of the documents, said: “We have long known that bacteria can perform the metabolic closure into unfavorable environments, transforming in long -lived indestructible latent spores that can survive for thousands of years.”
“This happens through asymmetric cell division, where the largest part, the ‘stem cell’, involves the smallest part, the ‘amateur’, providing nutrients and a protective outer layer. Continue to build protective layers around its genetic materials until it is ready to be released as spore.”
While this process is well understood, the mechanisms behind the closure of metabolism have remained a mystery until scientists discovered that a previously not characterized protein called MDFA was behind it.
Professor Isaacson explained: “Each cell has a ‘recycling center’ called protease, responsible for decomposing old or damaged proteins. We discover that MDFA, a protein that we did not know the function of previously, acts as an adapter that recruits proteins to recycle.
“In the case of sporulation, this protein instructs the cell to get rid of its metabolic enzymes responsible for active growth, for destruction through protease, thus performing the part of the metabolic sporulation of sporulation.”
Once MDFA was identified, King’s chemicals were able to solve the crystalline structure of the protein using X -ray crystallography, revealing a completely new molecular shape. This has allowed them to better understand how MDFA joins a part of the recycling channel in the cells, a protein called Clpc.
The scientists also found that when they forced the cells to grow happily to overexpress MDFA, it became toxic to the cells and exploded.
While the MDFA is not present in most other forms of bacteria, CLPC and the recycling machine, so they can be similar protected behind the sporulation in other bacteria, including those that cause diseases.
Professor Isaacson said: “This discovery has improved our understanding of how bacteria operates and opens a new way of exploring sporulation. Since sporulation plays a key role in the survival of bacteria, we more understand this process, we can control and eliminate the harmful bacterium.”
Scientists also expect their findings to lead to new strategies to develop antimicrobials.
Professor Isaacson added: “If you can aim at cell degradation machinery to eliminate particular proteins, this can open new paths for antimicrobial therapies, similar to an emerging form of cancer treatment, known as degradation or protca of directed proteins, which reuses the recycling system of a cell for therapy.”