Towards a Rigorous Network of Protein-Protein Interactions of the Model Sulfate Reducer Desulfovibrio vulgaris Hildenborough
2011

Protein-Protein Interactions in Desulfovibrio vulgaris

Sample size: 134 publication 10 minutes Evidence: high

Author Information

Author(s): Chhabra Swapnil R., Joachimiak Marcin P., Petzold Christopher J., Zane Grant M., Price Morgan N., Reveco Sonia A., Fok Veronica, Johanson Alyssa R., Batth Tanveer S., Singer Mary, Chandonia John-Marc, Joyner Dominique, Hazen Terry C., Arkin Adam P., Wall Judy D., Singh Anup K., Keasling Jay D.

Primary Institution: Lawrence Berkeley National Laboratory

Hypothesis

Can we reconstruct a reliable protein-protein interaction network for Desulfovibrio vulgaris using affinity purification and mass spectrometry?

Conclusion

The study successfully identified a high-confidence network of protein-protein interactions in Desulfovibrio vulgaris, revealing significant metabolic features and potential regulatory mechanisms.

Supporting Evidence

  • The study identified 134 high-confidence protein-protein interactions.
  • Biological replicates were used to enhance the reliability of the interaction data.
  • The interactions were validated through comparative and functional genomics analyses.
  • Statistical tests were applied to assign confidence to each putative interacting pair.

Takeaway

Scientists studied how proteins in a tiny bacteria called Desulfovibrio vulgaris interact with each other to understand how they work together.

Methodology

Affinity purification followed by mass spectrometry was used to identify protein-protein interactions.

Potential Biases

The reliance on specific tagging methods may introduce biases in the interaction data.

Limitations

The study's approach may not capture all interactions due to the limitations of the affinity purification method and potential false positives.

Statistical Information

P-Value

p<0.001

Statistical Significance

p<0.001

Digital Object Identifier (DOI)

10.1371/journal.pone.0021470

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication