Van Ingen Group

Molecular basis of chromatin function

Research in the group of Hugo van Ingen focusses primarily on the molecular basis of chromatin function. We are mostly interested in the interactions of histone proteins and nucleosomes with other chromatin factors such as chaperones, remodelers or proteins that control epigenetics. Using a combination of state-of-the-art NMR, biochemical and computational methods, we aim to decipher the structural basis of nucleosome recognition as well as the role protein motions herein. We aspire to create a new perspective on protein-nucleosome complexes, afforded by the unique sensitivity of NMR spectroscopy to structure, dynamics and interactions. We apply and develop new approaches to tackle these challenging systems. Next to the nucleosome-focused research, we also engage in collaborative projects ranging from protein interaction studies to NMR theory.


first generation team!

PhD students: Ivan Corbeski (joined with prof. dr. Rolf Boelens), Velten Horn, Ulric le Paige, Clara van Emmerik, Heyi Zhang & Vincenzo Lobbia

Key publications:

  • V. Horn*, M. Uckelmann*, H. Zhang, J. Eerland, I. Aarsman, U.B. le Paige, C. Davidovich, T.K. Sixma and H. van Ingen (2019). Structural basis of specific H2A K13/K15 ubiquitination by RNF168. Nat. comm., 10, doi:10.1038/s41467-019-09756-z.
  • C.L.van Emmerik and H. van Ingen (2019). Unspinning chromatin: revealing the dynamic nucleosome landscape by NMR. Prog.NMR Spectr.,110,1-19.
  • S. Xi*, U.B. le Paige*, M. Baldus, and H. van Ingen (2018). Site-specific studies of nucleosome interactions by solid-state NMR spectroscopy. Angew. Chem. Int. Ed. Engl., 57, p. 4571-4575.
  • R. van Nuland, F.M.A. van Schaik, M. Simonis, S. van Heesch, E. Cuppen, R. Boelens, M. Timmers and H. van Ingen(2013). Nucleosomal DNA binding drives the recognition of H3K36 methylated nucleosomes by the PSIP1-PWWP domain. Epigenetics & Chromatin, 6, 12-24. 
  • H. Kato*,H. van Ingen*, B.-R. Zhou*, H. Feng, M. Bustin, L.E. Kay and Y. Bai (2011). Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR. Proc. Natl. Acad. Sci. USA, 108, 12283-12288.