Matthieu Gagnon
University of Texas Medical Branch at Galveston, TX·Biochemistry
Ribosomes are the cell's protein-making machines. They read messenger RNA (mRNA) instructions with the help of transfer RNAs (tRNAs) and protein helpers called translation factors.
- Fields
Biochemistry
Biophysics
Microbiology & Immunology
- Topics
ribosome
protein synthesis
translation
- Grants
- 1 known grant, through Apr 2030
What they work on
- 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.
- Define how initiation factors IF1 and IF2 act on ribosomes that are already making proteins to trigger peptidyl-tRNA drop-off. This drop-off releases the unfinished protein chain still attached to its tRNA.
- Explain how elongation factor 4 (EF-4) and ABCF proteins reshape the tRNA and the growing protein chain inside the ribosome to rescue stalled ribosomes and give bacteria antibiotic resistance.
More about the research
Mistakes and stalls during this process waste energy and can produce faulty proteins, so cells rely on quality-control systems. Bacterial ribosomes are also the target of most antibiotics used in hospitals. Learning how they check their own work could therefore reveal new ways to fight infections.
Why it matters
Most hospital antibiotics target the bacterial ribosome. Knowing how bacteria check protein-making quality and rescue stalled ribosomes, including how ABCF proteins help bacteria resist antibiotics, could point to new targets for antimicrobial drugs. This could help in treating bacterial infections.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Alexander S Mankin
University of Illinois Chicago, IL·Microbiology & Immunology
Optimize small-molecule inhibitors of peptidyl-tRNA hydrolase, the bacterial enzyme that recycles unfinished protein chains, by synthesizing derivatives of sub-micromolar hits for stronger activity against the Klebsiella pneumoniae enzyme and better uptake into cells.
Jailson Brito Querido
University of Michigan, MI·Biochemistry
Determine how expanded GGGGCC repeats in C9orf72 mRNA physically engage the ribosome to trigger non-AUG start site selection, using cryo-electron microscopy with biochemical and genetic approaches.
Jamie H Cate
University of California-Berkeley, CA·Biochemistry
Determine how eIF3, a translation start factor, and partner proteins interact with structured RNA elements to switch translation of specific mRNAs on or off, using molecular and structural approaches.
The school
University of Texas Medical Branch at Galveston: 14 labs on PI Pages, $241M a year on research, 141 research doctorates a year.
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