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    Spatiotemporal regulation of Heterochromatin Protein 1-alpha oligomerization and dynamics in live cells.

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    Author
    Hinde, E; Cardarelli, F; Gratton, E
    Date
    2015-08-04
    Source Title
    Scientific Reports
    Publisher
    Springer Science and Business Media LLC
    University of Melbourne Author/s
    Hinde, Elizabeth
    Affiliation
    School of Physics
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Hinde, E., Cardarelli, F. & Gratton, E. (2015). Spatiotemporal regulation of Heterochromatin Protein 1-alpha oligomerization and dynamics in live cells.. Sci Rep, 5 (1), pp.12001-. https://doi.org/10.1038/srep12001.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/256849
    DOI
    10.1038/srep12001
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4523856
    Abstract
    Heterochromatin protein 1 (HP1) is a central factor in establishing and maintaining the heterochromatin state. As consequence of playing a structural role in heterochromatin, HP1 proteins can have both an activating as well as repressive function in gene expression. Here we probe how oligomerisation of the HP1-α isoform modulates interaction with chromatin, by spatially resolved fluorescence correlation spectroscopy (FCS). We find from fluctuation analysis of HP1-α dynamics that this isoform exists as a dimer around the periphery of heterochromatin foci and these foci locally rotate with characteristic turn rates that range from 5-100 ms. From inhibition of HP1-α homo-oligomerization we find the slow turn rates (20-100 ms) are dimer dependent. From treatment with drugs that disrupt or promote chromatin compaction, we find that HP1-α dimers spatially redistribute to favor fast (5-10 ms) or slow (20-100 ms) turn rates. Collectively our results demonstrate HP1-α oligomerization is critical to the maintenance of heterochromatin and the tunable dynamics of this HP1 isoform.

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