A Bridge Too Far: How Dps Protein From E. coli Condenses DNA

Learn about bacterial DNA protection mechanisms in this 33-minute seminar presentation exploring how Dps protein from E. coli interacts with and condenses DNA. Discover the fascinating world of bacterial stress responses as the speaker delves into the structure and function of Dps, a dodecameric protein with ferroxidase activity. Explore cutting-edge single molecule condensation assays and mathematical modeling using the Ising model to understand the hysteresis in DNA-protein interactions. Gain insights into how different DNA topologies affect Dps binding rates and the formation of condensed structures, with special attention to the protein's preference for supercoiled DNA. Part of the Biological Physics/Physical Biology seminar series, this talk bridges molecular biology and physics to explain fundamental bacterial survival mechanisms.

Syllabus

Intro
Life is hard for single celled organisms.
Stressed bacteria produce Dps, a DNA binding protein
Dps is a dodecamer (12mer) with a ferroxidase enzymatic function
Dps protects bacteria in times of stress
Single molecule condensation assay
Ising model can explain hysteresis
We can identify different topologies in the
Dps binds with different rates to different toplog
Ising-like cooperativity gives single condensed structure
Why does Dps prefer supercoiled DNA