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Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase

来自 Semantic Scholar

阅读量：

76

作者：

R Bransteitter，P Pham，MD Scharff，MF Goodman

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摘要：

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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关键词：

DNA Deaminase Unmarried RNA AID Artificial insemination by donor

DOI：

10.1073/pnas.0730835100

被引量：

1359

年份：

2003

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来源期刊

Proceedings of the National Academy of Sciences
2003/04/01

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2004
被引量：125

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