About

My research focuses on the structural and biophysical basis of protein–chromatin interactions that control gene expression and cell fate. Using cryo-EM, NMR spectroscopy, and quantitative binding approaches, I study how transcription factors recognize and modify nucleosomes. My current work centers on a plant bHLH transcription factor complex that carries an intrinsic histone methyltransferase domain — structurally derived from bacterial metabolic enzymes — capable of both reading and writing histone marks. I am determining the structural architecture of this complex bound to modified nucleosomes, characterizing its non-SET catalytic mechanism, and mapping how its dual reader-writer activity shapes chromatin during developmental fate transitions. More broadly, I am interested in how protein domain architecture encodes multifunctional activity at the chromatin interface and how these mechanisms can be applied to synthetic epigenetic engineering.

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