Hong Jin
University of Illinois Urbana-Champaign, IL·Biochemistry
Ribosomes are the cell's protein-making machines. In the crowded inside of a cell they sometimes pause, stall or even crash into one another.
- Fields
Biochemistry
Biology
Microbiology & Immunology
- Topics
Drg
developmentally regulated GTP-binding protein
GTPase
- Grants
- 1 known grant, through May 2027
What they work on
- Determine how the conserved GTPase Drg affects paused ribosomes, using test-tube translation systems rebuilt from E. coli and yeast to probe the peptidyl transferase center and measure peptide bond formation rates.
- Map the proteins Drg interacts with in E. coli and S. cerevisiae cells using APEX proximity labeling, which tags nearby proteins in living cells.
- Test which identified Drg interactions are important for its function in translation using mutagenesis and biochemical studies.
More about the research
Some pauses are planned, giving a new protein time to fold or reach its destination. Others are harmful errors. How cells tell the two apart, and how stuck ribosomes recover and keep working, is unclear. This project studies Drg, an ancient GTPase (an enzyme that switches on and off by binding and breaking down the energy molecule GTP). Drg has evolved alongside the ribosome and recent findings suggest it may act as a general helper of translation, the process of building proteins.
Why it matters
The work adds basic understanding of how cells keep protein production running when ribosomes pause or stall, and how they balance protein synthesis and quality. Because Drg is conserved from bacteria to yeast, the principles found could eventually inform understanding of gene expression control across living organisms.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Amy MacQueen
Wesleyan University, CT·Genetics
Define how the N terminus of Zip1, a synaptonemal complex building block, works with the Zip3 SUMO ligase to promote crossover recombination in budding yeast, using structure-function genetic analysis.
Matthieu Gagnon
University of Texas Medical Branch at Galveston, TX·Biochemistry
Determine how release factor 3 (RF3) releases protein chains from ribosomes that have made errors and helps protein folding during synthesis, using cryo-EM structures of bacterial 70S ribosome complexes.
Rachel Niederer
University of Michigan, MI·Biochemistry·Early-career
Directly measure ribosome recruitment on thousands of 5′-UTR sequences, the leader regions of mRNAs, that are used differently in cancer cells, to identify functional RNA elements.
The school
University of Illinois Urbana-Champaign: 41 labs on PI Pages, $907M a year on research, 870 research doctorates a year.
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