Functional requirements of AID's higher order structures and their interaction with RNA-binding proteins.

@article{Mondal2016FunctionalRO,
  title={Functional requirements of AID's higher order structures and their interaction with RNA-binding proteins.},
  author={Samiran Mondal and Nasim Ara Begum and Wenjun Hu and T. Honjo},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2016},
  volume={113 11},
  pages={E1545-54}
}
Activation-induced cytidine deaminase (AID) is essential for the somatic hypermutation (SHM) and class-switch recombination (CSR) of Ig genes. Although both the N and C termini of AID have unique functions in DNA cleavage and recombination, respectively, during SHM and CSR, their molecular mechanisms are poorly understood. Using a bimolecular fluorescence complementation (BiFC) assay combined with glycerol gradient fractionation, we revealed that the AID C terminus is required for a stable… CONTINUE READING
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