Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide
2009
Protein Interaction in Mycobacterium tuberculosis
publication
Evidence: moderate
Author Information
Author(s): Saurabh Garg, Md Suhail Alam, Richa Bajpai, Kishan KV Radha, Pushpa Agrawal
Primary Institution: Department of Environmental and Biomolecular Systems, OGI School of Science and Engineering, Oregon Health and Science University
Hypothesis
The study aims to identify the substrate protein(s) of Mycobacterium tuberculosis WhiB1.
Conclusion
The study concludes that GlgB is a substrate of WhiB1, which reduces its intra-molecular disulfide bond.
Supporting Evidence
- WhiB1 was identified as a thioredoxin-like protein that interacts with GlgB.
- The interaction was confirmed through yeast two-hybrid screening and GST pull-down assays.
- Mass spectrometry showed that GlgB has an intra-molecular disulfide bond between C193 and C617.
Takeaway
This study found that a protein called WhiB1 helps another protein, GlgB, by changing its structure to work better.
Methodology
The study used yeast two-hybrid screening and GST pull-down assays to identify and confirm the interaction between WhiB1 and GlgB.
Digital Object Identifier (DOI)
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