SFB 1064

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A16 - Metabolic coupling of histone modification during chromatin assembly

We would like to test why proteasomal activity is required for the binding of metabolic enzymes to chromatin and whether the metabolic enzymes cooperate with the pro-teasome to stimulate histone modification. We will focus on two enzymes of the C1 metabolism, the Drosophila SAM-Synthetase, SAM-S and the Adenosylhomocysteinase AHCY13, which are most strongly affected by proteasome inhibition. Our study will shed light on the mechanisms that mediate the coupling of metabolic processes and chromatin assembly and lay the groundwork for a better understanding of the role of cellular metabolism and proteostasis as a global effector of chromatin structure and function.


Figure: STRING network of proteins interacting with chromatin during in vitro assembly

Imhof, Axel

Prof. Dr. Axel Imhof

Biomedical Center - Molecular Biology, LMU Munich

+49 (0)89 2180 - 75420