Nature: Scientists have successfully developed a functional proteomic blueprint for E. coli that promises to reveal the function and interoperability of different genes in cells

December 14, 2020 // -- Understanding how genes work and how they interact with another gene is a major goal that scientists working on biology want to achieve, and of course, this can pose enormous challenges in terms of both methods and the number of experiments required, and recent research has changed scientists' ability to map gene function and interaction. In a study published in the international journal Nature, researchers from the European Molecular Biology Laboratory and others developed an innovative technique to measure the activity of thousands of genes at the same time;
picture source: Savitski Team, Holly Joynes/EMBL Thermal Proteomics Analysis reveals the function of bacterial cell proteins At the heart of this study is thermal proteomic analysis (TPP, thermal proteome profiling), a technique developed in 2014 by researcher Michail Savitski and his team, based on the principle that exposure to heat promotes the structural breakdown of proteins, a phenomenon researchers call "denature", in which proteins become insoluble, which turns into solids when the egg is boiled.
The researchers used this TPP method in live E. coli, heating cells to different temperatures to analyze how much of each protein in each cell at each temperature is soluble, the temperature of protein denaturation, or to tell researchers whether a protein is in an active state or can interact with a drug or another protein, because the structure of the protein changes when involved in any interaction, and the different structures of the same protein require varying degrees of heat before denaturation. In the
article, the researchers conducted the experiment on 121 E. coli mutants, each with a footprint removed, and then used TPP technology to conduct a deep analysis of the mutants and observe how all proteins in cells are expressed and how they denature, and the results may help researchers analyze the function and interaction of each protein, including hundreds of proteins that scientists do not currently know about.
The dilemma of essential proteins Is currently commonly used by researchers to study a single protein by removing the genes that encode the protein and monitoring the effects of culling on cell behavior, but such methods cannot be used to study the necessary proteins, the genes on which cells depend, because the absence of these genes can contribute to cell death.
'The technology used by the researchers represents another big step forward in the future for scientists to study the function of essential proteins,' said researcher Dr. Andr? Mateus. 'We found that while the levels of these proteins did not change in the mutants we studied (a trait that makes it difficult for researchers to study the function of proteins by measuring gene expression), their thermal stability often changes.'
stability of the necessary proteins may change, perhaps due to changes in their activity.
although the study was conducted in E. coli, the most studied bacterial species by scientists, the researchers hope to apply similar research techniques in other lesser-understood organisms later. one of the goals of the
researchers is to conduct research in the human gut microbiome, a special ecosystem that forms all the microbes in the gut, which is a key direction of the researchers' future research plans, and more and more studies are now showing that the gut microbiome is closely related to human health and disease, and that it is closely related to the functioning of the human brain and even how the body's immune system functions properly.
() Originals: Mateus, A., Hevler, J., Bobonis, J.et al. The functional proteome landscape of Escherichia coli. Nature (2020).doi:10.1038/s41586-020-3002-5。