Müller

Scientists led by Jürg Müller at the MPI of Biochemistry have deciphered a read-write mechanism that influences the expression of our genes. more

Scientists use mass spectrometry to determine the absolute copy number of nuclear proteins and histone marks to advance our understanding how the fruit fly embryo develops. more

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

Many proteins in our cells are decorated with sugar molecule add-ons, which are essential for the functions of these proteins. One particular type of sugar modification, called GlcNAc, is of key importance, because our cells cannot survive without it. Researchers at the Max Planck Institute of Biochemistry in Martinsried near Munich have recently uncovered a previously unknown mechanism explaining how this sugar residue affects protein function and thereby influences our development. These results have been published in the journal Developmental Cell. more

The packaging of DNA by histone proteins into chromatin regulates many processes, including the decision of whether genes are transcribed or whether they are silent. The addition of specific chemical tags on histone proteins mark genes as being silenced.  One of these tags is the covalent linkage of a small protein called ubiquitin to one of the histones. This modification was discovered more than 30 years ago but its molecular function has remained elusive. Scientists of the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany now identified a protein complex that binds this ubiquitin modification and show how this is connected to gene silencing. more