Professor John Schwabe - Department of Molecular and Cell Biology (formerly Biochemistry), Henry Wellcome Laboratories of Structural Biology, University of Leicester
23rd January 2017 at 12:00pm [Download iCalendar / .ics file]
My research group seeks to understand the molecular mechanisms that underlie the epigentic reprogramming of the genome during cellular differentiation and development. Our particular interest is in Histone Deacetylase (HDAC) complexes whose primary role is to remove acetyl groups from lysine sidechains within the tails of histone proteins resulting in hypo-acetylated chromatin that is associated with inactive or repressed genes.
There are at least five classes of HDAC-containing complexes that are targeted to chromatin. These contain the class I HDACs 1, 2 or 3 along with a variety of other proteins that target the complex to chromatin and/or possess other enzymatic activities. Importantly, the enzymatic activity of the HDACs requires assembly into these complexes.Our structural and functional studies have given insight into the assembly and mechanism of action of these complexes. The crystal structure of HDAC3 in complex with its cognate co-repressors SMRT revealed, quite unexpectedly, that this complex is regulated by inositol phosphate. Studies of further HDAC complexes suggests that such regulation is a common theme. We are also exploring the assembly of several entire HDAC complexes and are beginning to understand their mode of assembly and the cross-talk between different components.
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