Activation-Induced Cytidine Deaminase Shuttles between Nucleus and Cytoplasm like Apolipoprotein B mRNA Editing Catalytic Polypeptide 1

Activation-induced cytidine deaminase (AID) is a molecule central to initiating class switch recombination, somatic hypermutation, and gene conversion of Ig genes. However, its mechanism to initiate these genetic alterations is still unclear. AID can convert cytosine to uracil on either mRNA or DNA...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2004-02, Vol.101 (7), p.1975-1980
Main Authors: Ito, Satomi, Nagaoka, Hitoshi, Shinkura, Reiko, Begum, Nasim, Muramatsu, Masamichi, Nakata, Mikiyo, Honjo, Tasuku
Format: Article
Language:English
Subjects:
3T3 cells
AIDS
Amino Acid Sequence
Amino acids
Animals
APOBEC-1 Deaminase
apolipoprotein B
B lymphocytes
B-Lymphocytes - cytology
B-Lymphocytes - metabolism
Biological Sciences
Cell lines
Cell Nucleus - metabolism
Cells, Cultured
Cytidine Deaminase - chemistry
Cytidine Deaminase - genetics
Cytidine Deaminase - metabolism
Cytoplasm
Cytoplasm - metabolism
DNA
Enzymes
Humans
Immunology
Messenger RNA
Mice
Molecular Sequence Data
Mutation
NIH 3T3 Cells
Nuclear Localization Signals
Peptides
Protein Structure, Tertiary
Protein Transport
Proteins
Ribonucleic acid
RNA
RNA editing
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Summary:Activation-induced cytidine deaminase (AID) is a molecule central to initiating class switch recombination, somatic hypermutation, and gene conversion of Ig genes. However, its mechanism to initiate these genetic alterations is still unclear. AID can convert cytosine to uracil on either mRNA or DNA and is involved in DNA cleavage. Although these events are expected to take place in the nucleus, overexpressed AID was found predominantly in the cytoplasm. Here, we demonstrated that AID is a nucleocytoplasmic shuttling protein with a bipartite nuclear localization signal and a nuclear export signal in its N and C termini, respectively. In addition to previously identified genetic, structural, and biochemical similarities of AID with apolipoprotein B mRNA editing catalytic polypeptide 1, an RNA editing enzyme of ApoB100 mRNA, the present finding provides another aspect to their resemblance, suggesting that both may have homologous reaction mechanisms.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0307335101