Scientists at IMBA in Vienna have identified the final component that turns the RNA ligase into a fully viable enzyme in humans. That opens up perspectives for new treatment strategies for numerous types of breast cancer and leukemia.
Ligases are enzymes that aid the bonding of two molecules. For example, the RNA ligase ensures that copied parts of DNA are bonded into a viable tRNA, which in turn delivers the blueprint for producing proteins.
New starting point for cancer treatment
RNA ligases also have other functions that have not yet been researched in depth in humans because the composition of this important enzyme was not clear. “We already know from studies on yeasts that ligases are involved in defending cells from stress factors,” said Javier Martinez, a group leader at IMBA.
These functions are highly probable in mammal cells as well, and could be a new starting point for cancer therapies – especially for the treatment of various types of breast cancer and leukemia. Scientists already believe there is a close relationship between the function of the enzyme and the onset of these diseases.
“If we target and block one part of the ligase function, we will be able to approach cancer therapy in a much more specific manner than before. The impact of this enzyme is much farther down the cell’s signal transduction cascade than conventional medicinal targets,” said Martinez. This can be compared to a tree with one leaf affected by a disease. Of course it would be possible to cut off a thick limb to get rid of the diseased leaf. But it would be far less damaging to the tree to cut off just one thin branch.
This new approach is highly promising, and will certainly attract the interest of the pharmaceutical industry. But first Javier Martinez wants to test the function of ligases in mice.
Fundamental component of biology identified
This research into the function of ligases and their role in fighting cancer was made possible by the work of Martinez’ team, in which the entire composition of ligase was resolved piece by piece. The researchers’ initial success came in 2011, when they were first able to describe the most important basic components of the enzyme (Popow et al., Science 2011).
Now Johannes Popow, a young, gifted scientist, has achieved a breakthrough, which the renowned scientific journal Nature has published in its current issue. He discovered that an important protein called archease is bonded to the ligase. Without this protein, the enzyme can catalyze only one single bonding process. Archease is what makes it possible for the enzyme to regenerate so it is ready for the next catalyzation process.
Popow is very pleased “that we have identified this crucial component, and that by understanding the composition of ligase we will now be able to examine the function of this important enzyme more closely, and possibly apply the results for medical science.”
J. Popow, J. Jurkin, A. Schleiffer, J. Martinez. Analysis of orthologous groups reveals Archease and DDX1 as tRNA splicing factors. Nature, 2014. DOI 10.1038/nature13284.
Evelyn Devuyst | idw - Informationsdienst Wissenschaft
Pathogenic bacteria hitchhiking to North and Baltic Seas?
22.07.2016 | Alfred-Wegener-Institut, Helmholtz-Zentrum für Polar- und Meeresforschung
Unconventional quasiparticles predicted in conventional crystals
22.07.2016 | Max-Planck-Institut für Chemische Physik fester Stoffe
Researchers at the U.S. Department of Energy's (DOE) Ames Laboratory have discovered an unusual property of purple bronze that may point to new ways to achieve high temperature superconductivity.
While studying purple bronze, a molybdenum oxide, researchers discovered an unconventional charge density wave on its surface.
Munich Physicists have developed a novel electron microscope that can visualize electromagnetic fields oscillating at frequencies of billions of cycles per second.
Temporally varying electromagnetic fields are the driving force behind the whole of electronics. Their polarities can change at mind-bogglingly fast rates, and...
Breakup of continents with two speed: Continents initially stretch very slowly along the future splitting zone, but then move apart very quickly before the onset of rupture. The final speed can be up to 20 times faster than in the first, slow extension phase.phases
Present-day continents were shaped hundreds of millions of years ago as the supercontinent Pangaea broke apart. Derived from Pangaea’s main fragments Gondwana...
Scaffolding and specialised workers help with the delivery – Heidelberg biochemists gain new insights into biogenesis
A type of scaffolding on which specialised workers ply their trade helps in the manufacturing process of the two subunits from which the ribosome – the protein...
Scientists at the Helmholtz Zentrum München have developed a new mass spectrometry imaging method which, for the first time, makes it possible to analyze hundreds of metabolites in fixed tissue samples. Their findings, published in the journal Nature Protocols, explain the new access to metabolic information, which will offer previously unexploited potential for tissue-based research and molecular diagnostics.
In biomedical research, working with tissue samples is indispensable because it permits insights into the biological reality of patients, for example, in...
15.07.2016 | Event News
15.07.2016 | Event News
11.07.2016 | Event News
25.07.2016 | Physics and Astronomy
25.07.2016 | Materials Sciences
25.07.2016 | Materials Sciences