William Childers
University of Pittsburgh, PA·Microbiology & Immunology
Bacteria have no membrane-bound organelles, yet they still sort their internal chemistry into compartments. They do this with biomolecular condensates, droplets of protein and RNA that form much as oil separates from water.
- Fields
Microbiology & Immunology
Biochemistry
Biophysics
- Topics
biomolecular condensates
phase separation
BR-bodies
- Grants
- 1 known grant, through Apr 2030
What they work on
- Test how copper and oxidative stress drive BR-bodies from liquid to solid through cysteine cross-links in RNase E, and whether this protects PNPase and aconitase, using live-cell experiments, test-tube assays and a redox-sensitive fluorescent biosensor.
- Screen a focused library of cysteine-reactive small molecules for compounds that dissolve BR-bodies, as a foundation for antimicrobial discovery.
- Determine whether ATP depletion, cytoplasmic acidification and polyphosphate accumulation solidify BR-bodies and suppress RNA decay in stationary phase and acid stress, using biosensors, targeted mutants and in vitro reconstitution.
- Test whether stress-induced co-localization of BR-bodies with the PopZ condensate, a cell-cycle regulator, affects chromosome segregation or RNA decay.
More about the research
This project studies how one such droplet helps bacteria survive harsh conditions. That question matters both for basic cell biology and for finding new ways to kill bacteria.
Why it matters
Bacterial infections are increasingly hard to treat, and this work looks for weak points in how bacteria cope with stresses like copper, oxidation and acid. Small molecules that dissolve BR-bodies could become a starting point for new antibiotic strategies that target bacterial stress responses rather than classic drug targets.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Jiahui Wu
University of Massachusetts, MA·Biochemistry
Develop an RNA tag with ultrahigh affinity to accurately identify the RNA-binding proteins that make up ribonucleoprotein complexes and trigger condensate formation.
Ned Wingreen
Princeton University, NJ·Biophysics
Determine how flow, changes over time and biofilm spatial structure shape the strategies bacteria use to gather and act on quorum-sensing information carried by autoinducer signal molecules.
Jeroen Roelofs
University of Kansas, KS·Biochemistry
Determine how proteasome-associated assembly factors, including Pba1-Pba2/PAC1-PAC2, Fub1/PI31, and Blm10/PA200, contribute to sequential versus parallel pathways during the early assembly of new proteasome complexes.
The school
University of Pittsburgh: 83 labs on PI Pages, $1.5B a year on research, 403 research doctorates a year.
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