期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 11, 页码 E1545-E1554出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1601678113
关键词
AID; BiFC; hnRNP U; SERBP1; APOBEC
资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [17002015, 24590352]
- Human Frontier Science Program (HFSP)
- Grants-in-Aid for Scientific Research [15H05784, 24590352, 16K07214, 22000015] Funding Source: KAKEN
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 dimer formation. Furthermore, AID monomers and dimers form complexes with distinct heterogeneous nuclear ribonucleoproteins (hnRNPs). AIDmonomers associate with DNA cleavage cofactor hnRNP K whereas AID dimers associate with recombination cofactors hnRNP L, hnRNP U, and Serpine mRNA-binding protein 1. All of these AID/ribonucleoprotein associations are RNA-dependent. We propose that AID's structure-specific cofactor complex formations differentially contribute to its DNA-cleavage and recombination functions.
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