How a Bacterial Protein Stimulates DNA Unwinding
Author Information
Author(s): Feng Cui, Sunchu Bharath, Greenwood Mallory E, Lopper Matthew E
Primary Institution: University of Dayton
Hypothesis
Can a bacterial PriB with weak single-stranded DNA binding activity stimulate the DNA unwinding activity of its cognate PriA helicase?
Conclusion
A bacterial PriB homolog with weak single-stranded DNA binding activity can stimulate the DNA unwinding activity of its cognate PriA helicase.
Supporting Evidence
- N. gonorrhoeae PriA's helicase activity is similar to that of E. coli PriA.
- N. gonorrhoeae PriB can stimulate PriA's helicase activity despite its weak DNA binding.
- PriB's ability to stimulate ATP hydrolysis by PriA is a novel finding not observed in E. coli.
Takeaway
This study shows that a protein called PriB, which doesn't bind DNA very well, can still help another protein, PriA, unwind DNA, which is important for bacteria to copy their DNA.
Methodology
The study used fluorescence polarization spectroscopy to examine the interactions between PriA, PriB, and various DNA structures, along with assays to measure helicase and ATPase activities.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website