Our lab is interested in how genetic material is packaged in eukaryotes and the implications this has for biological processes. Within each cell of our body, we have nearly four metres of DNA distributed over 46 chromosomes which is sequestered in a nucleus of only 1000 m3. Chromatin must, therefore, fulfil two conflicting roles: structure DNA so that genomic instability is minimised, but at the same time remain accessible to factors involved in transcription, replication and repair. In studying these contrary roles, our investigations span two length scales, namely the assembly of individual nucleosomes to form the 10 nm fibre and the mechanics of higher-order chromatin domains. To do this we utilise both in vitro biochemical approaches and advanced live-cell imaging.
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 J.R., Bowman A.J. (2018) Evidence for the nuclear import of histones H3.1 and H4 as monomers.
EMBO J. doi:10.15252/embj.201798714.
Bowman, A., Koide, A., Goodman, J.S., Colling, M.E., Zinne, D., Koide, S., and Ladurner, A.G. (2017). sNASP and ASF1A function through both competitive and compatible modes of histone binding.
Nucleic Acids Res 45, 643-656.
Bowman, A., Lercher, L., Singh, H.R., Zinne, D., Timinszky, G., Carlomagno, T., and Ladurner, A.G. (2016). The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats.
Nucleic Acids Res 44, 3105-3117.