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dc.contributor.authorHinde, E
dc.contributor.authorPandzic, E
dc.contributor.authorYang, Z
dc.contributor.authorNg, IHW
dc.contributor.authorJans, DA
dc.contributor.authorBogoyevitch, MA
dc.contributor.authorGratton, E
dc.contributor.authorGaus, K
dc.date.accessioned2021-02-04T01:08:50Z
dc.date.available2021-02-04T01:08:50Z
dc.date.issued2016-03-01
dc.identifierpii: ncomms11047
dc.identifier.citationHinde, E., Pandzic, E., Yang, Z., Ng, I. H. W., Jans, D. A., Bogoyevitch, M. A., Gratton, E. & Gaus, K. (2016). Quantifying the dynamics of the oligomeric transcription factor STAT3 by pair correlation of molecular brightness. NATURE COMMUNICATIONS, 7 (1), https://doi.org/10.1038/ncomms11047.
dc.identifier.issn2041-1723
dc.identifier.urihttp://hdl.handle.net/11343/259275
dc.description.abstractOligomerization of transcription factors controls their translocation into the nucleus and DNA-binding activity. Here we present a fluorescence microscopy analysis termed pCOMB (pair correlation of molecular brightness) that tracks the mobility of different oligomeric species within live cell nuclear architecture. pCOMB amplifies the signal from the brightest species present and filters the dynamics of the extracted oligomeric population based on arrival time between two locations. We use this method to demonstrate a dependence of signal transducer and activator of transcription 3 (STAT3) mobility on oligomeric state. We find that on entering the nucleus STAT3 dimers must first bind DNA to form STAT3 tetramers, which are also DNA-bound but exhibit a different mobility signature. Examining the dimer-to-tetramer transition by a cross-pair correlation analysis (cpCOMB) reveals that chromatin accessibility modulates STAT3 tetramer formation. Thus, the pCOMB approach is suitable for mapping the impact oligomerization on transcription factor dynamics.
dc.languageEnglish
dc.publisherNATURE PUBLISHING GROUP
dc.titleQuantifying the dynamics of the oligomeric transcription factor STAT3 by pair correlation of molecular brightness
dc.typeJournal Article
dc.identifier.doi10.1038/ncomms11047
melbourne.affiliation.departmentBiochemistry and Molecular Biology
melbourne.affiliation.departmentSchool of Physics
melbourne.affiliation.facultyCollected Works
melbourne.source.titleNature Communications
melbourne.source.volume7
melbourne.source.issue1
dc.rights.licenseCC BY
melbourne.elementsid1053844
melbourne.contributor.authorBogoyevitch, Marie
melbourne.contributor.authorHinde, Elizabeth
dc.identifier.eissn2041-1723
melbourne.accessrightsOpen Access


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