Robert McGinty
University of North Carolina at Chapel Hill, NC·Biochemistry
Every cell packs about two meters of DNA into its nucleus by wrapping it around histone proteins. Each wrapped unit is called a nucleosome, and chains of nucleosomes form chromatin.
- Fields
Biochemistry
Biophysics
Genetics
- Topics
chromatin
nucleosome
histones
- Grants
- 1 known grant, through May 2029
What they work on
- Define how combinations of histone post-translational modifications recruit reader proteins across the proteome, using designer nucleosomes with chemically defined modification patterns in interactome screens.
- Determine near-atomic resolution structures of histone-modification writers, readers and erasers bound to nucleosomes, and test the resulting mechanisms with structure-guided mutations in cell models.
- Uncover how large multi-subunit chromatin complexes coordinate several enzymatic activities to regulate gene expression, combining structural biology, biochemistry, biophysics, cell biology and genomics.
- Determine how the Anaphase Promoting Complex, a cell-cycle ubiquitin ligase, acts on chromatin to control gene expression and histone homeostasis.
More about the research
Chemical tags on histones, called post-translational modifications (PTMs), act as signals that help decide which genes turn on, when DNA is copied and how damage is repaired. Enzymes known as writers add these tags, erasers remove them, and reader proteins recognize them. When this signaling goes wrong, it contributes to cancer and developmental disorders. Still, it is largely unknown how these enzymes work on actual nucleosomes, or how combinations of tags recruit readers to specific places in the genome.
Why it matters
Cancer and developmental disorders often involve broken chromatin signaling. By showing how histone-modifying enzymes and readers recognize nucleosomes, this work could reveal how the system is hijacked in disease. Near-atomic structures could provide starting points for drugs that target chromatin regulators and support functional studies in disease models.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Marcey Waters
University of North Carolina at Chapel Hill, NC·Chemistry
Determine how amino acid sequence controls structure and self-assembly of coiled-coil peptides, rope-like bundles of protein helices, into nanospheres and fibrils, including the roles of positive and negative cooperativity.
David Morgan
University of California-San Francisco, CA·Biochemistry
Determine how cyclin-dependent kinases (Cdks), enzymes that tag proteins with phosphates, build complex multisite phosphorylation patterns on their substrates in the eukaryotic cell cycle, using biochemical approaches.
Qingfei Zheng
Purdue University, IN·Biochemistry
Develop chemical probes that selectively label and enrich different histone monoaminylations, such as serotonylation and dopaminylation of histone H3 at glutamine 5 (H3Q5).
The school
University of North Carolina at Chapel Hill: 72 labs on PI Pages, $1.6B a year on research, 523 research doctorates a year.
Reach out
A start for your email. Fill in the brackets.