Gerbich Therese M.

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Gerbich
First Name
Therese M.
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  • Preprint
    mRNA structure determines specificity of a polyQ-driven phase separation
    ( 2018-04) Langdon, Erin M. ; Qiu, Yupeng ; Ghanbari Niaki, Amirhossein ; McLaughlin, Grace A. ; Weidmann, Chase ; Gerbich, Therese M. ; Smith, Jean A. ; Crutchley, John M. ; Termini, Christina M. ; Weeks, Kevin M. ; Myong, Sua ; Gladfelter, Amy S.
    RNA promotes liquid-liquid phase separation (LLPS) to build membrane-less compartments in cells. How distinct molecular compositions are established and maintained in these liquid compartments is unknown. Here we report that secondary structure allows mRNAs to self-associate and determines if an mRNA is recruited to or excluded from liquid compartments. The polyQ-protein Whi3 induces conformational changes in RNA structure and generates distinct molecular fluctuations depending on the RNA sequence. These data support a model in which structure-based, RNA-RNA interactions promote assembly of distinct droplets and protein-driven, conformational dynamics of the RNA maintain this identity. Thus, the shape of RNA can promote the formation and coexistence of the diverse array of RNA-rich liquid compartments found in a single cell.
  • Article
    Phosphoregulation provides specificity to biomolecular condensates in the cell cycle and cell polarity
    (Rockefeller University Press, 2020-07-06) Gerbich, Therese M. ; McLaughlin, Grace A. ; Cassidy, Katelyn ; Gerber, Scott ; Adalsteinsson, David ; Gladfelter, Amy S.
    Biomolecular condensation is a way of organizing cytosol in which proteins and nucleic acids coassemble into compartments. In the multinucleate filamentous fungus Ashbya gossypii, the RNA-binding protein Whi3 regulates the cell cycle and cell polarity through forming macromolecular structures that behave like condensates. Whi3 has distinct spatial localizations and mRNA targets, making it a powerful model for how, when, and where specific identities are established for condensates. We identified residues on Whi3 that are differentially phosphorylated under specific conditions and generated mutants that ablate this regulation. This yielded separation of function alleles that were functional for either cell polarity or nuclear cycling but not both. This study shows that phosphorylation of individual residues on molecules in biomolecular condensates can provide specificity that gives rise to distinct functional identities in the same cell.