Now, researchers at the University of Michigan, along with colleagues in Belgium, have discovered a new antioxidant system that protects single cysteines. The research appears in the Nov. 20 issue of the journal Science.
Our body's proteins, which are made up of amino acids and perform essential roles, can be injured by reactive species known as oxidants. Over time, the injuries can lead to cancer, heart disease, Alzheimer's disease and other serious medical conditions. To guard against such harm, our cells have special proteins that can repair or reverse oxidative damage. But until now, no such repair system had been identified for single cysteines, which are particularly susceptible to the damage.
In the current research, U-M's Kate Carroll and colleagues used previously developed chemical probes to investigate and nail down the mechanism involved.
"Our results reveal that a protein called DsbG serves this precise function in the periplasmic compartment in bacteria, protecting single cysteines residues from hyperoxidation and inactivation," said Carroll, an assistant professor of chemistry and a research assistant professor in the Life Sciences Institute. The periplasmic compartment is a space between the inner and outer membranes of bacteria such as Escherichia coli, which were used in this study. Although human cells have no periplasmic compartment, they have an equivalent membrane network called the endoplasmic reticulum.
"Since proteins from the DsbG family are widespread and have been identified in the majority of genomes including humans, some of these related members may play similar roles in controlling cysteine oxidation," Carroll said. A better understanding of these biological processes may lead to more effective antioxidant therapies.
Carroll's coauthors on the paper are Matthieu Depuydt, Katleen Denoncin and Jean-François Collet of the Université catholique de Louvain and the Brussels Center for Redox Biology; University of Michigan graduate student Stephen Leonard; Didier Vertommen and Pierre Morsomme of the Université catholique de Louvain; and Khadija Wahni and Joris Messens of Vrije Universiteit Brussel and Brussels Center for Redox Biology.
Nancy Ross-Flanigan | Newswise Science News
Plankton swim against the current
12.12.2017 | Schweizerischer Nationalfonds SNF
To differentiate or not to differentiate?
12.12.2017 | Max-Planck-Institut für Biologie des Alterns
Tiny pores at a cell's entryway act as miniature bouncers, letting in some electrically charged atoms--ions--but blocking others. Operating as exquisitely sensitive filters, these "ion channels" play a critical role in biological functions such as muscle contraction and the firing of brain cells.
To rapidly transport the right ions through the cell membrane, the tiny channels rely on a complex interplay between the ions and surrounding molecules,...
The miniaturization of the current technology of storage media is hindered by fundamental limits of quantum mechanics. A new approach consists in using so-called spin-crossover molecules as the smallest possible storage unit. Similar to normal hard drives, these special molecules can save information via their magnetic state. A research team from Kiel University has now managed to successfully place a new class of spin-crossover molecules onto a surface and to improve the molecule’s storage capacity. The storage density of conventional hard drives could therefore theoretically be increased by more than one hundred fold. The study has been published in the scientific journal Nano Letters.
Over the past few years, the building blocks of storage media have gotten ever smaller. But further miniaturization of the current technology is hindered by...
With innovative experiments, researchers at the Helmholtz-Zentrums Geesthacht and the Technical University Hamburg unravel why tiny metallic structures are extremely strong
Light-weight and simultaneously strong – porous metallic nanomaterials promise interesting applications as, for instance, for future aeroplanes with enhanced...
An interdisciplinary group of researchers interfaced individual bacteria with a computer to build a hybrid bio-digital circuit - Study published in Nature Communications
Scientists at the Institute of Science and Technology Austria (IST Austria) have managed to control the behavior of individual bacteria by connecting them to a...
Physicists in the Laboratory for Attosecond Physics (run jointly by LMU Munich and the Max Planck Institute for Quantum Optics) have developed an attosecond electron microscope that allows them to visualize the dispersion of light in time and space, and observe the motions of electrons in atoms.
The most basic of all physical interactions in nature is that between light and matter. This interaction takes place in attosecond times (i.e. billionths of a...
11.12.2017 | Event News
08.12.2017 | Event News
07.12.2017 | Event News
11.12.2017 | Physics and Astronomy
11.12.2017 | Earth Sciences
11.12.2017 | Information Technology