Priya R. Banerjee
University at Buffalo, NY·Biophysics·Early-career
Cells organize much of their chemistry without using membranes. Proteins and RNA can separate out of the surrounding liquid into dense droplets, much the way oil beads up in water, forming compartments called biomolecular condensates that concentrate specific molecules and keep others out.
- Fields
Biophysics
Biochemistry
Genetics
- Topics
biomolecular condensates
liquid-liquid phase separation
pioneer transcription factors
- Grants
- 2 known grants, through Aug 2029
What they work on
- Test whether pioneer transcription factors, proteins that can bind DNA packed into closed chromatin, act by forming liquid-like droplets on DNA that concentrate RNA polymerases and nucleosome-remodeling complexes to switch genes on.
- Determine the physical rules governing phase separation of pioneer transcription factors and how co-condensation with DNA and cofactors tunes their gene-regulatory activity.
- Probe the interior environment and physical aging of condensates inside living cells by combining fluorescence lifetime imaging, which reports local surroundings from dye glow times, with optical-tweezer nanorheology.
- Map how RNA drives phase separation coupled to percolation, and test the hypothesis that RNA-binding proteins act as chaperones that block RNA from locking into irreversible networks.
- Decode sequence grammars in disordered prion-like protein domains that encode selective interactions among transcription factors, coactivators and chromatin remodelers, and manipulate them to control condensate composition.
More about the research
These droplets are not simply liquid: they behave like viscoelastic materials, flowing on some timescales and resisting deformation on others, and some of them harden over time into solid-like clumps resembling those found in neurodegenerative disease. Work here asks what physical rules decide when such droplets form, what they are made of, how stiff or fluid they are, and how those material properties feed back on two central cellular jobs: switching genes on and handling RNA.
Why it matters
Hardened protein and RNA assemblies are a recurring feature of neurodegenerative disorders, and faulty condensates are also implicated in cancer. By measuring what makes these droplets fluid, what makes them age into solids, and which sequences decide who joins them, this work could identify the molecular steps that go wrong in disease and point to places where that transition might be blocked or reversed.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Lin Guo
Thomas Jefferson University, PA·Biochemistry
Determine how the nuclear import receptor Kapβ2 engages and chaperones newly found partner proteins that lack a nuclear localization signal, using cryo-electron microscopy to solve their structures.
Jiahui Wu
University of Massachusetts, MA·Biochemistry
Develop an RNA tag with ultrahigh affinity to accurately identify the RNA-binding proteins that make up ribonucleoprotein complexes and trigger condensate formation.
John Straub
Boston University, MA·Biophysics
Identify factors that govern liquid-liquid phase separation and later amyloid aggregation of the disordered proteins tau and alpha-synuclein, combining experiments with computer simulations.
The school
University at Buffalo: 32 labs on PI Pages, $542M a year on research, 316 research doctorates a year.
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