Andrew Bowman | Chromatin Dynamics
"To quantify is not to be a scientist, but goodness, it does help."
- P. B. Medawar (Advice to a Young Scientist)
Dr. Andrew Bowman became an independent QBP fellow following postdoctoral work in the Laboratory of Andreas Ladurner (Ludwig-Maximilians-University Munich) and a PhD under the supervison of Tom Owen-Hughes (University of Dundee, UK).
Since the discovery of histone chaperones nearly four decades ago, much effort has gone into understanding how they function. The prevailing view is that histones must pass through a number of different chaperoning complexes that favour their thermodynamic incorporation into nucleosomes and prevent non-specific aggregation. To date this has mostly been approached by looking at individual chaperones in isolation.
My goal is to accurately model the process of nucleosome assembly at the systems level through quantifying dynamic transitions that occur within the histone chaperoning pathway. This approach relies on the ability to make quantitative measurements of the histone chaperoning network in live cells using novel synthetic approaches combined with live-cell microscopy.
Smith MJ & Bowman AJ. Observation of histone nuclear import in living cells: implications in the processing of newly synthesised H3.1 & H4. BioRxiv (Preprint) - https://doi.org/10.1101/111096
Bowman A. et al., sNASP and ASF1A function through both competitive and compatible modes of histone binding. Nucleic Acids Res. (2017) 45(2):643-656
Bowman A. et al., The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats.
Nucleic Acids Res. (2016) 44:3105-3117
Bowman A. et al., The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. Nucleic Acids Res. (2014) 42:6038-51
Bowman A. et al., The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation.
Molecular Cell (2011) 41:398-408