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Andreas Ladurner    Welcome to our Department!

The research groups in our department investigate the nuclear processes that allow organisms to react and adapt to a variety of environmental changes. We are interested in the identification and analysis of novel mechanisms that dynamically regulate chromatin structure and transcription, with a keen focus on the role of cellular metabolites, DNA damage, signalling networks and mitochondrial function.
We study how aging, DNA damage, and animal behaviour condition gene activity and nuclear function.

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    Congratulations to Magdalena Murawska for obtaining a Marie Skłodowska-Curie Individual Fellowship from the Research Fellowship Programme programme of the European Union. The 24-months postdoctoral fellowship will allow Magdalena to do identify novel regulators and interactors for the chaperone FACT that target its functions to heterochromatin using functional genomics and proteomics.

  • Aurelio Nardozza_xs_2014
    Our post-doctoral fellow Aurelio Nardozza was recently awarded with the prestigious Marie Skłodowska-Curie Individual Fellowship from the Research Fellowship Programme programme of the European Union. He will get funding for his research in our department for 24 months.

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    In this issue of Cell Reports (Cell Reports, October 2013) we describe the development and the validation of a novel and broadly applicable biochemical procedure: CAST-ChIP (chromatin affinity purification from specific cell types by chromatin immunoprecipitation). CAST-ChIP powerfully identifies cell-type-specific as well as cell-type-invariant chromatin states, enabling the systematic dissection of chromatin structure and gene regulation within complex tissues such as the brain. Our study identifies H2A.Z as an active chromatin signature that is refractory to changes across cell fates.

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    In the June issue of Cell (Cell, 6 June 2013), we report crystal structures of full-length Drosophila Cryptochrom (dCRY), a dCRY loop deletion construct, and the photolyase homology region of mouse CRY1. We show that the FAD and antenna chromophore-binding regions, a predicted coiled-coil helix, the C-terminal lid, and charged surfaces are involved in FAD-independent mPER2 and FBXL3 binding and mCLOCK/mBMAL1 transcriptional repression. The structure of a mammalian cryptochrome1 protein may catalyze the development of CRY chemical probes and the design of therapeutic metabolic modulators.
    Additional information: LMU press release, June 07, 2013

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    In this Nature Letter (Nature, 2013), we report the crystal structure of the evolutionarily conserved FACT chaperone domain Spt16M in complex with the H2A–H2B heterodimer, shedding light on how the complex promotes the activity of enzymes that require nucleosome reorganization.
    Additional information: LMU press release, May 23, 2013
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    In two studies (Nature Structural & Molecular Biology, 2013; The EMBO Journal, 2013), we identify crucial enzymes that are involved in the process of quickly alerting the cellular defense and repair system. We describe a family of macrodomain enzymes present in viruses, yeast and animals that reverse cellular ADP-ribosylation by acting on mono-ADP-ribosylated substrates.
    More information: LMU press release, March 12, 2013