Press releases - News from the MPI of Biochemistry

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The genetic transmission of gene locks

March 16, 2017
Although all cells in an organism contain the same genes, only some of the genes are activated in a given cells and others remain inactive. Genes coil around histone proteins in the form of DNA threads. If a gene has to remain inactive, its histones are marked by the PRC2 enzyme so that this gene is locked down and cannot be read. When cells divide and the genes are copied, these histone marks must be placed again, at exactly the same location. The mechanism that enables transmission of this information has now been explained by Jürg Müller from the Max Planck Institute of Biochemistry in Martinsried in a study published in the journal Science. [more]
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ERC Grant for Naoko Mizuno

March 15, 2017
Naoko Mizuno, head of the research group “Cellular and Membrane Trafficking” at the Max-Planck-Institute of Biochemistry in Martinsried, has been awarded a Consolidator Grant by the European Research Council (ERC). [more]
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Nobel Prize Laureate Robert Huber turns 80

February 17, 2017
 “Proteins are nice, crystals are nicer”  “Photosynthesis is the most important chemical reaction on Earth.” So proclaimed the Royal Swedish Academy of Sciences in 1988 in its announcement that Robert Huber, together with Hartmut Michel and Johann Deisenhofer, was to receive the Nobel Prize for Chemistry. Working as a team, they decoded the three-dimensional structure of the photosynthetic reaction centre. The Nobel Laureate and head of the “Structural Research” emeritus working group at the Max Planck Institute (MPI) of Biochemistry celebrates his 80th birthday on February 20. The fascination for the structure of proteins has never left him. Currently, he is researching drugs to treat autoimmune diseases.  [more]
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Johann-Georg-Zimmermann Medal for Axel Ullrich

February 06, 2017
Axel Ullrich, Professor Emeritus of the Department of Molecular Biology at the Max Planck Institute of Biochemistry in Martinsried has been awarded the Johann-Georg-Zimmermann Medal for his services in the field of cancer research. For more than 40 years the award, sponsored by Deutsche Hypothekenbank AG, has recognized outstanding scientists in the field of cancer research. The MHHplus Foundation will present the award at Hannover Medical School on 6 February 2017. [more]
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With scissors and string – chromosome segregation in meiosis  

January 13, 2017
Once together, never apart – isn’t that how the saying goes? Not so in meiosis, the special type of cell division in which gametes, sperm and egg cells are formed. At the start of meiosis the ring-shaped protein complex, referred to as cohesin, is the string that ties the chromosome strands together. The chromosomes are where the blueprint for the body is stored. If each egg cell and each sperm is to come out of meiosis with only one set of chromosomes, these strings need to be cut up in a precise pattern. Scientists from the Max Planck Institute of Biochemistry have demonstrated in baker’s yeast how a kinase enzyme, which is also present in the human body, controls the cleavage of the cohesin rings and coordinates it with the exit from meiosis and gamete formation. It is a mechanism, which could explain how chromosome segregation is regulated, or goes wrong, in human sperm and egg cells. [more]
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The internal clock of cells orchestrates 25 percent of all protein switches

January 10, 2017
Circadian is the latin meaning for “about a day”. Circadian clocks have evolved to adapt our lives to the daily environmental changes on earth: light and warmth during the day and darkness and cold at night. Scientists at the Max-Planck-Institute of Biochemistry in Martinsried discovered with the help of the mass spectrometry, that more than 25 percent of the molecular protein switches in mouse liver cells change in a daily manner. These rhythmic switches are binding sites for phosphate molecules, that regulate the function of proteins, and thereby the daily metabolic processes in the organ. The study was published in the journal Cell Metabolism. [more]
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RNA jam in molecular 3D printer – SKI complex helps

December 22, 2016
Although the terms “cryo-EM” and “SKI complex” evoke images of ice and snow, they actually relate to structural biology. Scientists at the Max Planck Institute of Biochemistry and the Gene Center of the University of Munich (LMU) have now shown that the cellular protein factory and the SKI protein complex are in direct contact. The SKI complex is part of a molecular shredder that breaks down mRNA, the construction manual for proteins, into its individual components. To conduct their analysis, the researchers used cryo-electron microscopy, a technique that involves flash-freezing protein complexes to allow even the tiniest details of their structure to be studied in their natural state. [more]
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