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Independent Fellows

Andrew Bowman | Chromatin Dynamics

bowman.pngUPDATE: We are excited to announce that Andrew has been awarded of a Sir Henry Dale Fellowship from the Wellcome-Trust and Royal Society to continue his exciting research programme

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 supervision 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 by 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.

Lab page | Pubmed |


Selected reading

- Pardal A.J., Fernandes-Duarte F., Bowman A.J. (2019)The histone chaperoning pathway: from ribosome to nucleosome. Essays Biochem. 63(1):29-43. (Review)

- Apta-Smith M.J., Hernandez-Fernaud JR, Bowman A.J. Evidence for the nuclear import of histones H3.1 and H4 as monomers. EMBO J. 2018, doi: 10.15252/embj.201798714.

- Bowman A. et al., sNASP and ASF1A function through both competitive and compatible modes of histone binding. Nucleic Acids Res. 2017, doi: 10.1093/nar/gkw892.
- 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, doi: 10.1093/nar/gkv1372.
- Bowman A. et al., The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. Nucleic Acids Res. 2014, doi: 10.1093/nar/gku232.
- Bowman A. et al., The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation.
Molecular Cell 2011, doi: 10.1016/j.molcel.2011.01.025.

Irene Stefanini | Evolutionary Systems Biology


Dr. Irene Stefanini became an independent QBP fellow following postdoctoral work with Dr. Claudio Donati (Fondazione Edmund Mach, San Michele all'Adige, Italy) and a PhD under the supervision of Prof. Cavalieri (University of Florence, Italy).

The yeast Saccharomyces cerevisiae is one of the most studied microorganisms, used as model system to provide crucial insights into fundamental cellular processes and human diseases at the molecular level. However, research has been largely limited to a single atypical laboratory strain.

With the ever-increasing number of sequenced genomes and natural S. cerevisiae isolates I now aim to exploit the natural biodiversity to obtain insights on the predictability of phenotypic response from individual genomic sequences.

Lab page | Pubmed | ORCID


Selected reading

- Brilli M., Trabocchi A., Weil T., Cavalieri D., Stefanini I. Relations between Effects and Structure of Small Bicyclic Molecules on the Complex Model System Saccharomyces cerevisiae. Front. Pharmacol. 2017, doi: 10.3389/fphar.2017.00170.
- Stefanini I. et al., Social wasps are a Saccharomyces mating nest. Proc Natl Acad Sci U S A. 2016, doi: 10.1073/pnas.1516453113.
- Stefanini I. et al., Role of social wasps in Saccharomyces cerevisiae ecology and evolution. Proc Natl Acad Sci U S A. 2012, 10.1073/pnas.1208362109.
- Stefanini I. et al., A systems biology approach to dissection of the effects of small bicyclic peptidomimetics on a panel of Saccharomyces cerevisiae mutants. J. Biol. Chem. 2010, doi: 10.1074/jbc.M110.125153.