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Citation

Thesis Title
Histone H1 phosphorylation during mitosis

Read article at Massey Research Online:

To fit within the confines of the cell nucleus deoxyribonucleic acid (DNA) is complexed with histone proteins forming chromatin. The linker histone H1 binds strongly to DNA, compacting it so that chromosomes can be accurately segregated when a cell divides during mitosis. Phosphorylation is a modification of histone H1 that is laid down by Aurora B kinase, a master regulator of mitosis. During her research, Ms Bond mutated the Aurora B phosphorylation site within histone H1 resulting in an increased incidence of mitotic defects such as lagging and bridging chromosomes. Such aberrations during mitosis can lead to genetic instability and ultimately aneuploidy, a hallmark of cancer. Additionally, the interaction between histone H1 and proteins involved in condensing DNA throughout the cell cycle revealed that these interactions can be mediated through ribonucleic acid (RNA), indicating RNA may be important in forming high order chromatin structures.

Supervisors
Dr Tracy Hale
Professor Kathryn Stowell
Dr Helen Fitzsimons