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The red plaques are areas of DNA damage that are stabilized by proteins. Videographic: Microscopy of a cell (delimited with blue). Det betyder, at videoen Proteinstillads ikke kan afspilles. ‘This could be compared to putting a plaster cast on a broken leg it stabilizes the fracture and prevents the damage from getting worse and reaching a point where it can no longer heal,’ says Postdoc Fena Ochs, from the Novo Nordisk Foundation Center for Protein Research and the first author of the new study.ĭin internetbrowser understøtter ikke iframes. This technology enables researchers to zoom in on living cells and visualize objects about the size of one thousandth of the width of a hair and follow how the protective protein scaffold assembles and grows around the DNA fracture. Highly advanced super-resolution microscopes were used in this study. This opens up an opportunity to better design how DNA damage causes disease and design drugs that improve treatment of patients with unstable DNA,’ says Center Director and Professor Jiri Lukas of the Novo Nordisk Foundation Center for Protein Research. Understanding the body's natural defence mechanisms enables us to better understand how certain proteins communicate and network to repair damaged DNA. This scaffold then locally concentrates special repair proteins, that are in short supply, and that are critically needed to repair DNA without mistakes.Ĭlick on the graphic below to enlarge it.
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In short, two proteins called 53BP1 and RIF1 engage to build a three-dimensional ‘scaffold’ around the broken DNA strands. The findings have been published in the scientific journal Nature. Now researchers from the Novo Nordisk Foundation Center for Protein Research at the University of Copenhagen have discovered how certain proteins orchestrate repair of damaged DNA to ensure its stability over generations and to prevent collateral damage to the neighbouring unharmed DNA. In turn, this can lead to irreversible genetic damage and ultimately cause diseases such as cancer, immune deficiency, dementia or developmental defects. As a result, DNA strands can be broken at least once during each cell division cycle and this frequency can increase by certain lifestyles, such as smoking, or in individuals who are born with defects in DNA repair. This is not a small task because our DNA is constantly under attack, both from the environment but also from the cell’s own metabolic activities. Defects in the 3D-stabilizing process can lead to DNA damage running wild before it can be repaired.Įvery day, the body's cells divide millions of times, and the maintenance of their identity requires that a mother cell passes complete genetic information to daughter cells without mistakes.Other proteins from the so-called Shieldin network are then attracted to actually repair the damage. Researchers from the University of Copenhagen have now demonstrated that DNA damage in normal cells is quickly stabilised by the proteins 53BP1 and RIF1.Flaws in these mechanisms can be disastrous and are a hallmark of many types of cancer.Fortunately, our cells are designed to monitor, care for and repair the DNA to protect the organism from permanent damage.The worst damages are the so-called DNA double-strand break fractures, where both ends of the DNA break apart. Every day, both internal and external factors damage the DNA in our cells.In humans, a DNA molecule is approximately 2 metres long when uncoiled but is presently compressed in the nucleus of every cell.DNA is the template of life and contains the recipe for our body’s building blocks, the proteins.Our model provides new insights into chromosome higher order structure. We therefore propose a new structural model of the chromosome scaffold that includes twisted double strands, consistent with the physical properties of chromosomal bending flexibility and rigidity. This reversion to the original morphology underscores the role of the scaffold for intrinsic structural integrity of chromosomes. We also find that scaffold protein can adaptably recover its original localization after chromosome reversion in the presence of cations. Here, we use three dimensional-structured illumination microscopy (3D-SIM) and focused ion beam/scanning electron microscopy (FIB/SEM) to reveal the axial distributions of scaffold proteins in metaphase chromosomes comprising two strands. However, the organization and function of the scaffold are still controversial. The most important structural finding has been the presence of a chromosome scaffold composed of non-histone proteins so-called scaffold proteins.
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Chromosome higher order structure has been an enigma for over a century.