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Genschere schaltet ich with eengebauten Timer ab

Genschere schaltet ich with eengebauten Timer ab

CRISPR Genscheren, as a new tool of molecular biology, has its origins in a specific, bacterial immune system. If a virus attack has arisen, it is worth making them disappear. Researchers of the University Hospital Bonn (UKB) and the University of Bonn, in collaboration with the Researchers of the Pasteur Institute in France, have hired a time switch integrated in the Genscheren, with the Genscheren itself switched can. The study origins have been published in the revised specialist journal “Nucleic Acids Research”.

A bakery has an antweed in the background, so that the CRISPR technology is activated. This bacterial immune system knows the disease of Phagen, which protects it from the fear of the Viren. The Type III variables that the immune system sets when spraying Phagen with zyklischen oligoadenylates (cOAs) bone substances her, with the Help the bacteria of a complex Notfallplan-anschallen. If you do that, a virus is optimal and the front is conquered can. A research team of PD Dr. Gregor Hagelueken from the Institute for Structural Biology at the UKB, the member in the Transdisciplinary Research Area (TRA) “Life & Health” as well as in the Excellence Cluster ImmunoSensation2 from the University of Bonn, the von der Genschere restored Bone substance cA4 and a protein name CalpL-bindet have been discovered. The so active protein has disappeared from a signal stream, which cancels the viral rage.

The Bonn researchers have developed a new aspect of the CRISPR system, which is very good for the biotechnological and medical swimming programs. “This new CRISPR-activated protein shear is a brand new work in the construction of molecular biology”, says Niels Schneberger, a doctoral candidate at the University of Bonn at the Institute for Structural Biology in the UKB, of one of the Discovery of CalpL Proteins that is enormously extensive.

Zellary action during the treatment of antiviral reactions

“If a viral fear is separated, the oligoadenylate is eliminated, an antiviral reaction is created and the Zelle in a normal life will be dissolved,” says Sophie Binder, who starts the first study with Schneberger and is the doctoral candidate of the University of Bonn at the Institute for Structural Biology of the UKB. The Bonn researchers are now working in collaboration with the researchers of the Institut Pasteur in Paris and the Kekulé Institutes for Organic Chemistry and Biochemistry of the University of Bonn, which the SAVED domain of CalpL protease has a ring nuclease activity, the cA4 spatter. “The protein is also taken up as a molecular timer, the immunoreaction abschaltet. While the ablation of cA4 in linear fragments while the protection against the immune system was regulated, a control check over the normal conditions was possible,” says Binder.

A scalable protease with CalpL is one of the biotechnological analyses of great interest. You can use the device if a molecular sensor is installed. “Everything is a new kind of Ring Nuclease Activation for the only Purpose or hindrance”, says PD Dr. Hagelueken. “In our study it may be that the man who does Ring Nuclease activation, can be so that the sensor is no longer made by himself. “

Support and security settings:
The project is being carried out by the Deutsche Forschungsgemeinschaft (DFG) and the Open Access Publication Fund of the University of Bonn. Next to the Institute for Structural Biology in the UKB, the Kekulé Institute for Organic Chemistry and Biochemistry of the University of Bonn and the Institut Pasteur, Paris, France, are cooperating in the study.

Publication: Sophie C. Binder, Niels Schneberger, Marianne Engeser, Matthias Geyer, Christophe Rouillon, Gregor Hagelueken: The SAVED domain of the type III CRISPR protease CalpL is a ring nuclease; Nucleic Acids Research,
DOI: 10.1093/nar/gkae676/7737999