Fields of Research

Peptide chemistry

Protein post-translational modifications

Chromatin structure and function

Regulation of the tumor suppressor protein p53

Biomolecular condensation

Research Summary

The Chatterjee lab studies the regulation of human chromatin structure and function by post-translational modifications of core histone proteins and the tumor suppressor protein p53. Trainees in the lab gain expertise in developing and applying novel chemical and biochemical tools to elucidate the effects of methylation, acetylation, ubiquitylation and sumoylation on gene transcription by RNA polymerase II, and to study the biochemical relationships, or crosstalk, between these modifications in histones and p53.

Research Statement

Reversible enzymatic modifications of protein side-chains, also known as post-translational modifications or PTMs, confer complexity to biological systems by dynamically regulating the location, structure, and activity of proteomes. Elucidating the mechanistic contributions of post-translationally modified proteins to key cellular processes, such as gene transcription, is critical for understanding normal human development and to identify new therapeutic targets in diseases arising from the misregulation of PTMs. To accomplish these goals, we are applying a seamless combination of chemical and molecular biological tools to investigate uniformly modified proteins in well-defined biophysical and biochemical systems. This enables us to elucidate the structure, function, and regulation of two important families of nuclear proteins – histones and transcription factors – that are implicated in cancers of the skin, breasts, lungs and brain.

Awards and Honors

NIGMS R35

Chemical Strategies To Investigate Biochemical Crosstalk In Human Chromatin