TatBC: Structural Units in the Twin Arginine Protein Transport System of Escherichia coli
2007
Understanding the TatBC Complex in E. coli
publication
Evidence: high
Author Information
Author(s): Orriss George L., Tarry Michael J., Ize Bérengère, Sargent Frank, Lea Susan M., Palmer Tracy, Berks Ben C.
Primary Institution: Department of Biochemistry, University of Oxford
Hypothesis
TatA is not required for the assembly or stability of the TatBC complex.
Conclusion
The study shows that TatC forms a stable core within the TatBC complex, independent of TatA.
Supporting Evidence
- TatB and TatC can form stable complexes without TatA.
- TatC forms a distinct multimeric complex independent of TatA and TatB.
- The predominant TatBC species has an apparent molecular weight of 430 kDa.
- TatC can form a stable core within the TatBC complex.
Takeaway
This research found that two proteins, TatB and TatC, can work together without needing a third protein, TatA, to stay stable.
Methodology
The study involved producing and characterizing TatB and TatC proteins, analyzing their complexes using blue native-PAGE and size exclusion chromatography.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website