Laboratory Robert Schneider


One of the major goals of post-genomic biology is to understand the molecular basis and physiological role of covalent protein modifications. We are using histones and the "histone code" as models to study multi-site protein modifications. Our aim is to identify new modifications, to decipher how these modifications are epigenetically inherited and how they can regulate gene expression and chromatin structure. The best studied examples for multi-site protein modifications are currently histone proteins. The complexity and diversity of histone (and other chromatin-associated) modifications add largely to the capacity of the genome to store and process information. We are currently only beginning to understand the many implications of this epigenetic information for biology and disease. Whilst it is still under discussion if histone modifications form a true "code", it has now been established that changes of histone modifications and of protein complexes binding to specific modifications are involved in the regulation of most - if not all - genes in eukaryotic cells. Therefore the significance of studying chromatin modifications extends far beyond the field of chromatin research, because changes in the modification pattern are likely to affect all biological processes.
Group Leader
1969
Born in Fuerstenfeldbruck, Germany
Undergraduate studies in Biology at the Ludwigs-Maximilians-University (LMU) Munich, Germany
1997-2000
PhD studies at the LMU Munich, Germany
2000-2004
Postdoctoral fellow at the Wellcome/Cancer Research UK Institute, Cambridge, UK
Since 2004
Group leader at the Max Planck Institute of Immunobiology and Epigenetics, Freiburg
Project Areas
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Novel Histone Modifications in the Control of Gene Expression and Chromatin Structure
The role of the histone code in gene regulation. Post-translational modification is a key mechanism regulating protein function. These modifications can be...
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The function of linker histone H1 modifications and variants
Currently the chromatin field is concentrating on core histone modifications. The linker histone H1 has an important function in establishing and maintaining...
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Functional characterisation of novel modifications in the core of the nucleosome
In addition to the histone tails, the central part of the nucleosome can also be modified. We have recently identified and characterised a new methylation...
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Recent Publications
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Chatting histone modifications in mammals.
Izzo A, Schneider R. (2010)
Brief Funct. Genomics 9, 429-443
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Histone H2A C-terminus regulates chromatin dynamics, remodeling and histone H1 binding.
Vogler, C., Huber, C., Waldmann, T., Ettig, R., Braun, L., Izzo, A., Daujat, S., Chassignet, I., Lopez-Contreras, A.J., Fernandez-Capetillo, O., Dundr, M., Rippe, K., Längst, G., and Schneider, R. (2010)
PLOS Genetics, e 1001234
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What an epigenome remembers.
Lange, U.C. and Schneider, R. (2010)
Bioassays 31, 859-866
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Going global - novel histone modifications in the globular domain of H3.
Tropberger, S. and Schneider, R. (2010)
Epigenetics 5, 112-117
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Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D.
Weiss, T., Hergeth, S., Zeissler, U., Izzo, A., Tropberger, P., Zee, B.M., Dundr, M., Garcia, B.A., Daujat, S. and Schneider, R. (2010)
Epigenetics Chromatin 3, 7
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Arginine methylation of the B-cell antigen receptor promotes differentiation.
Infantino, S., Waldmann, T., Benz, B., Jung, M., Schneider, R. and Reth, M. (2010)
Journal of Exp. Med. 207, 711-719
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H3 lysine 64 methylation is a novel heterochromatic mark dynamically remodelled during epigenetic reprogramming.
Daujat, S., Weiss, T., Mohn, F., Lange, U.C., Ziegler-Birling, C., Zeissler, U., Lappe, M., Schübeler, D., Torres-Padilla, M.E. and Schneider, R. (2009)
Nature Structural and Mol. Biol. 16, 777-781
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Novel tools to tackle protein acetylation.
Kamienariaz, K. and Schneider R. (2009)
Chem. & Biol. 16, 1027-1029
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Histone replacement underlies the process of epigenetic reprogramming in the mouse germ line.
Hajkova, P., Waldmann, T., Ancelin, K., Lange, U.C., Lacoste, N., Cesari, F., Lee, C., Almouzni, G., Schneider, R. and Surani, A. (2008)
Nature 452, 877-881
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The histone H1 family: specific members, specific functions.
Izzo, A., Kamienariaz, K. and Schneider, R. (2008)
Biol. Chem. 389, 333-343
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The multi-domain protein Brpf1, binds histones and is required for hox gene expression and segmental identity.
Laue, K., Daujat, S., Plaster, N., Roehl, H.H., Schneider, R. and Hammerschmidt, M. (2008)
Development 135, 1935-1946
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Normal germline establishment in mice carrying deleiton in the lfitm/Fragilis gene family cluster.
Lange, U.C., Adams, D.J., Lee, C., Barton, S., Schneider, R., Bradley A., and Surani A. (2008)
Mol. Cell. Biol. 15, 4688-4696
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