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School of Fundamental Sciences
College of Sciences
Untangling protein- G-quadruplex interactions in heterochromatin formation
The information encoded in our genomic DNA is intricately packaged inside of the cell nucleus via a DNA-protein complex called chromatin. This chromatin is packaged into highly compact domains known as heterochromatin, the process of which is regulated by the key architectural protein: Heterochromatin Protein 1α (HP1α). It is imperative that HP1α forms and maintains heterochromatin, as this compaction process is essential for both gene regulation and genomic stability, specifically at telomeres and centromeres of chromosomes. My research focusses on how HP1α is recruited to regions where heterochromatin must be maintained. Previously, I found that HP1α binds unique structures of DNA and RNA called G-quadruplexes (G4s), which we hypothesise are the factor which determine HP1α localisation and therefore compaction. My research goals are therefore to identify how HP1α interacts with G4s formed in vitro (as this is a very novel kind of interaction), and to determine how G4s alter the interaction of HP1α with chromatin. This structural research has significant applications in drug development to target G4-binding proteins or G4s of interest. The involvement of G4s in our genome is relatively unknown, but they have been implicated in regulation of cancer-associated genes, providing a target for future novel cancer drugs.
I come from Whanganui, New Zealand, a short trip away from Palmerston North.
Roach, R. J., Garavís, M., González, C., Jameson, G. B., Filichev, V. V., & Hale, T. K. (2019). Heterochromatin protein 1α interacts with parallel RNA and DNA G-quadruplexes. Nucleic Acids Research, 48(2), 682-693. 10.1093/nar/gkz1138
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Last updated on Tuesday 04 April 2017