Their research provides strong evidence that Flavin Adenine Dinucleotide (FAD) plays a structural role in the formation of tetrameric AidB. While their studies clearly show FAD-dependent oligomerization of AidB, they do not address whether FAD also has a catalytic function. However, the picture of AidB that is emerging invokes a role for the DNA-binding domain in localization of AidB to specific genes, while the protective function appears to reside elsewhere on the protein.
In future work, the collaborators will investigate whether this protective function resides with FAD or whether FAD was retained in the evolutionary process solely for its ability to stabilize the AidB tetramer.
This work was supported by National Institutes of Health Grants R01-GM072663 (to Sean Elliott) and P30-ES002109 (to Catherine Drennan) and National Science Foundation Grant MCB-0543833 (Drennan). Professor Drennan is a Howard Hughes Medical Institute Investigator.
The paper is available at http://pubs.acs.org/doi/full/10.1021/bi201340t, or click on the image below.