Göttingen Graduate School for Neurosciences, Biophysics, and Molecular Biosciences
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Fischle, Wolfgang, Dr.


Group Leader at the MPI for Biophysical Chemistry


  • Dr. rer. nat. (PhD), University of Tübingen, Germany, 2001

  • Graduate Research Fellow, The J. David Gladstone Institute (UCSF), San Francisco, CA, USA, 1997-2001

  • Postdoctoral Fellow, The Rockefeller University, New York, NY, USA, 2001-2005

  • Damon Runyon Cancer Research Fellow, 2002-2005

  • Independent Group Leader, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, since 2006




Major Research Interests

Chromatin is the physiological template of genetic information controlling the capacity of a cell’s genome to store, release, and inherit biological information. The fundamental unit of chromatin is the nucleosome: a stretch of DNA wrapped around a core of histone proteins (H2A, H2B, H3 and H4). Post-translational modifications of histones have emerged as key for regulating chromatin structure and are thought to crucially control chromatin dynamics and genome activity. Whereas more and more histone modification marks are being identified that alone or in combination could mediate distinct biological conditions of a cell and while correlative studies have begun to establish unambiguous links between several states of chromatin, various histone modifications, and diverse biological processes, our knowledge of how certain histone modifications exert their biological effects on a molecular/biochemical level is still very limited.

Due to their long-term stability, histone lysine methyl-marks are of particular interest to us, since they might be involved in establishing and maintaining durable and inheritable gene expression profiles (so called ‘epi-genetic’ regulation). Current projects include the study of Polycomb, HP1, and MBT proteins that bind to and act as effectors of distinct histone lysine methyl-marks. We are especially interested in the interplay of these factors and their cognate histone marks in regulating chromatin organization and dynamics. Furthermore, we are trying to identify and characterize novel binding proteins of various other histone modifications.

The long-term goal of our research is to gain mechanistic insight(s) into the signaling mechanisms and biological role of single but also combinations of histone modification marks and to understand how certain states of chromatin regulate the functionality of a cells genome. To this end, we aim to reconstitute chromatin-signaling pathways in recombinant and cell free systems and study their epi-genetic regulatory circuits in various biological model systems (i.e. Xenopus laevis, mice, tissue culture).



Homepage Department/Research Group

http://www.mpibpc.mpg.de/research/ags/fischle/



Selected Recent Publications

  • Seeliger D, Soeroes S, Klingberg R, Schwarzer D, Grubmüller H, Fischle W (2011) Quantitative Assessment of Protein Interaction with Methyl-Lysine Analogues by Hybrid Computational and Experimental Approaches. ACS Chem Biol]

  • Nikolov M, Stützer A, Mosch K, Krasauskas A, Soeroes S, Stark H, Urlaub H, Fischle W (2011) Chromatin Affinity Purification and Quantitative Mass Spectrometry Defining the Interactome of Histone Modification Patterns. Mol. Cell. Proteomics>

  • Koester-Eiserfunke N, Fischle W (2011) H3K9me2/3 Binding of the MBT Domain Protein LIN-61 Is Essential for Caenorhabditis elegans Vulva Development. PLoS Genet. 7:e1002017

  • Tsai WW, Wang Z, Yiu TT, Akdemir KC, Xia W, Winter S, Tsai CY, Shi X, Schwarzer D, Plunkett W, Aronow B, Gozani O, Fischle W, Hung MC, Patel DJ, Barton MC (2010) TRIM24 links recognition of a non-canonical histone signature to breast cancer. Nature 468:927-932

  • Franz H, Mosch K, Soeroes S, Urlaub H, Fischle W (2009) Multimerization and H3K9me3 binding is required for CDYL1b heterochromatin association. J. Biol. Chem. 284:35049-35059

  • Fischle W (2008) Talk is cheap-cross-talk in establishment, maintenance, and readout of chromatin modifications. Gen. Dev. 22:3375-3382

  • Zhang K, Mosch K, Fischle W, Grewal SI (2008) Roles of the Clr4 methyltransferase complex in nucleation, spreading and maintenance of heterochromatin. Nat. Struct. Mol. Biol. 15:381-388





  • GGNB Fischle

    Address
    Dr. Wolfgang Fischle
    Max Planck Institute
    for Biophysical Chemistry
    Chromatin Biochemistry Group
    Am Fassberg 11
    37077 Göttingen
    Germany

    Tel.: +49-(0)551-201 1340
    Fax: +49-(0)551-201 1197
    e-mail: wfischl@gwdg.de

    GGNB Affiliation
    Molecular Biology (IMPRS)
    Biomolecules: Structure - Function -
    Dynamics (GZMB)

    Molecular Biology of Microbial, Anim
    al and Plant Cells (GZMB)

    Genes and Development
    Physics of Biological and Complex S
    ystems (IMPRS)