Y. George Zheng
University of Georgia, GA·Biochemistry
Cells constantly fine-tune their proteins by attaching small chemical groups after the proteins are made. These changes are called post-translational modifications (PTMs).
- Fields
Biochemistry
Chemistry
Pharmacology
- Topics
post-translational modifications
protein methylation
protein methyltransferases
- Grants
- 2 known grants, through Jan 2028
What they work on
- Determine the molecular mechanisms and regulation of protein arginine methyltransferase (PRMT) activity, building on the lab's preliminary results.
- Characterize the activity, structure and function of little-studied protein methyltransferases, including those found in infectious pathogens.
- Develop modulators and probes selective for individual PRMT family members and use them to map PRMT-regulated cell pathways and disease processes.
- Investigate how protein methylation interacts with lysine acetylation to coordinate biological regulation.
- Develop chemical probes that label lysine methacrylylation and cysteine S-2-carboxypropylation, two proposed protein modifications derived from the valine metabolite methacrylyl-CoA.
- Map methacrylylated and S-2-carboxypropylated proteins across the human proteome using chemoproteomics and bioinformatics, then test how these modifications are controlled and what they do in cells.
More about the research
They can alter a protein's shape, activity, location in the cell and partners. They help control gene activity, cell division and signaling, and errors in them are linked to diseases such as cancer. Many PTMs are still poorly understood, and some have not yet been discovered. The lab uses chemical biology, which applies chemistry tools to biological questions, to study known PTMs and find new ones. It also designs molecules that could block disease-linked modifying enzymes.
Why it matters
Protein methyltransferases are overactive or mutated in cancer, inflammation, diabetes, neurological disorders and infection. Selective inhibitors from this work could become drug candidates for these conditions. Finding new modifications from valine metabolism would show how metabolism can directly change protein function. The new chemical probes would also give other researchers tools for studying the human proteome.
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.
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).
Kristofer Fritz
University of Colorado Denver/Anschutz Medical Campus, CO·Pharmacology
Characterize how chronic alcohol metabolism changes thiol redox signaling, the on-off switching of cysteine residues in proteins, in liver cells, using redox proteomics and bioinformatics.
The school
University of Georgia: 27 labs on PI Pages, $628M a year on research, 598 research doctorates a year.
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