College of Medicine
Bloom Lab
Led by Linda Bloom · Biochemistry and Molecular Biology
What we study
The Bloom Lab studies how proteins and DNA interact to copy and repair genomes. They use experiments to understand how replication machinery works and how it responds to DNA damage.
What working here is like
- Wet lab
- Bacteria & microbes
- Coding helps
- Projects
- 3
- Papers
- 5
Current projects
Mechanisms and Functions of Iron-Sulfur Helicases in DNA repair
Investigates how iron-sulfur helicases, proteins that unwind DNA, work in repairing damaged DNA, using biochemical experiments to understand how cells copy and fix their genomes.
Mechanisms of SSB in Coordinating DNA Replication and Repair
Exploring how single-stranded DNA binding protein coordinates replication and repair.
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Investigating the protein‑protein interaction of the Escherichia coli DinG helicase with single‑stranded DNA binding protein (SSB)
The lab mutated a single amino acid in the DinG helicase, produced the protein, and measured ATPase activity and DNA‑unwinding with and without SSB, finding reduced unwinding when SSB is present. The student carried out the mutagenesis and assays.
From the Spring 2025 UF Undergraduate Research Symposium · abstract book, p. 556
Summaries are written by AI in plain language from public symposium abstracts and may be imperfect.
Recent papers, explained
- A novel ψ–χ fusion protein for unravelling the contributions of χ to DNA replication and repair
2026 · Nucleic Acids Research
- The YoaA-χ helicase modulates the dynamics of single-stranded DNA binding protein on DNA
2025 · Nature Communications
Tests whether YoaA-χ helicase and SSB interact to help DNA damage tolerance.
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- Osmolyte influence on stability and oligomerization dynamics of the Saccharomyces cerevisiae PCNA sliding clamp
2024 · Biophysical Journal
- TheEscherichia coliclamp loader rapidly remodels SSB on DNA to load clamps
2022 · Nucleic Acids Research
Shows how SSB enhances clamp loader binding to DNA for replication.
- Characterization of the Escherichia coli XPD/Rad3 iron-sulfur helicase YoaA in complex with the DNA polymerase III clamp loader subunit chi (χ)
2022 · Journal of Biological Chemistry
Characterizes YoaA as an iron-sulfur helicase and studies its complex with χ.
Plain-language summaries are AI-written and reviewed by us; check the paper for details.
How to reach out
Linda Bloom hasn't set up this page yet. You can also look them up in the UF directory (search “Linda Bloom”).