The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase
Open accessAbstract
The expression of activation-induced cytidine deaminase (AID) is prerequisite to a “trifecta” of key molecular events in B cells: class-switch recombination and somatic hypermutation in humans and mice and gene conversion in chickens. Although this critically important enzyme shares common sequence motifs with apolipoprotein B mRNA-editing enzyme, and exhibits deaminase activity on free deoxycytidine in solution, it has not been shown to act on either RNA or DNA. Recent mutagenesis data in Escherichia coli suggest that AID may deaminate dC on DNA, but its putative biochemical activities on either DNA or RNA remained a mystery. Here, we show that AID catalyzes deamination of dC residues on single-stranded DNA in vitro but not on double-stranded DNA, RNA–DNA hybrids, or RNA. Remarkably, it has no measurable deaminase activity on single-stranded DNA unless pretreated with RNase to remove inhibitory RNA bound to AID. AID catalyzes dC → dU deamination activity most avidly on double-stranded DNA substrates containing a small “transcription-like” single-stranded DNA bubble, suggesting a targeting mechanism for this enigmatic enzyme during somatic hypermutation.
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Cites
Error-Prone Repair DNA Polymerases in Prokaryotes and Eukaryotes
Goodman, M. F. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.083101.124707 · Cited by 727
Self-citationDNA polymerase η is an A-T mutator in somatic hypermutation of immunoglobulin variable genes
Zeng, X., Winter, D. B., Kasmer, C., Kraemer, K. H., Lehmann, A. R., & Gearhart, P. J. (2001) · Nature Immunology · doi:10.1038/88740 · Cited by 420
Somatic mutation hotspots correlate with DNA polymerase η error spectrum
Rogozin, I. B., Pavlov, Y. I., Bebenek, K., Matsuda, T., & Kunkel, T. A. (2001) · Nature Immunology · doi:10.1038/88732 · Cited by 298
Cited by
Targeted nucleotide editing using hybrid prokaryotic and vertebrate adaptive immune systems
Nishida, K., Arazoe, T., Yachie, N., Banno, S., Kakimoto, M., Tabata, M., Mochizuki, M., Miyabe, A., Araki, M., Hara, K. Y., et al. (2016) · Science · doi:10.1126/science.aaf8729 · Cited by 1,349
Reversing DNA Methylation: Mechanisms, Genomics, and Biological Functions
Wu, H., & Zhang, Y. (2014) · Cell · doi:10.1016/j.cell.2013.12.019 · Cited by 1,065
“However, AID/APOBEC only efficiently acts on single-strand but not double-strand DNA (Bransteitter et al., 2003), and exhibit substantially lower activity on 5mC (10- to 20-fold) relative to cytosine, their canonical substrate (Nabel et al., 2012).”
Molecular Signals of Epigenetic States
Bonasio, R., Tu, S., & Reinberg, D. (2010) · Science · doi:10.1126/science.1191078 · Cited by 912
TETonic shift: biological roles of TET proteins in DNA demethylation and transcription
Pastor, W. A., Aravind, L., & Rao, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3589 · Cited by 897
The APOBEC Protein Family: United by Structure, Divergent in Function
Salter, J. D., Bennett, R. P., & Smith, H. C. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.05.001 · Cited by 408
Metadata
- Authors
- Bransteitter, R., Pham, P., Scharff, M. D., & Goodman, M. F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-03-21
- Volume
- 100
- Issue
- 7
- Pages
- 4102-4107
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2036806870
- Cited by
- 680
- References
- 3
- FWCI
- 20.16
- Type
- journal article
- Language
- en
- Open access
- green
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- Bransteitter, R., Pham, P., Scharff, M. D., & Goodman, M. F. (2003). Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0730835100
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