Evaluation of APOBEC3B Recognition Motifs by NMR Reveals Preferred Substrates

被引：9
作者：
Liu, Manjuan [1 ]
Mallinger, Aurelie [1 ]
Tortorici, Marcello [1 ]
Newbatt, Yvette [1 ]
Richards, Meirion [1 ]
Mirza, Amin [1 ]
van Montfort, Rob L. M. [1 ]
Burke, Rosemary [1 ]
Blagg, Julian [1 ]
Kaserer, Teresa [1 ]
机构：
[1] Inst Canc Res, Canc Res UK Canc Therapeut Unit, London SM2 5NG, England
来源：
ACS CHEMICAL BIOLOGY | 2018年 / 13卷 / 09期
关键词：
DNA CYTOSINE; CATALYTIC DOMAIN; STRUCTURAL BASIS; HUMAN CANCERS; DEAMINATION; MUTAGENESIS; RESTRICTION; MUTATION; BINDING;
D O I：
10.1021/acschembio.8b00639
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
APOBEC3B (A3B) deamination activity on ssDNA is considered a contributing factor to tumor heterogeneity and drug resistance in a number of human cancers. Despite its clinical impact, little is known about A3B ssDNA substrate preference. We have used nuclear magnetic resonance to monitor the catalytic turnover of A3B substrates in real-time. This study reports preferred nucleotide sequences for A3B substrates, including optimized 4-mer oligonucleotides, and reveals a breadth of substrate recognition that includes DNA sequences known to be mutated in drug-resistant cancer clones. Our results are consistent with available clinical and structural data and may inform the design of substrate-based A3B inhibitors.
引用
收藏
页码：2427 / 2432
页数：6
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