Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication

被引:533
作者
Ling, H
Boudsocq, F
Woodgate, R
Yang, W [1 ]
机构
[1] NIDDKD, Mol Biol Lab, NIH, Bethesda, MD 20892 USA
[2] NICHHD, Sect DNA Replicat Repair & Mutagenesis, NIH, Bethesda, MD 20892 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1016/S0092-8674(01)00515-3
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
Sulfolobus solfataricus P2 DNA polymerase IV [Dpo4) is a DinB homolog that belongs to the recently described Y-family of DNA polymerases, which are best characterized by their low-fidelity synthesis on undamaged DNA templates and propensity to traverse normally replication-blocking lesions. Crystal structures of Dpo4 in ternary complexes with DNA and an incoming nucleotide, either correct or incorrect, have been solved at 1.7 Angstrom and 2.1 Angstrom resolution, respectively. Despite a conserved active site and a hand-like configuration similar to all known polymerases, Dpo4 makes limited and nonspecific contacts with the replicating base pair, thus relaxing base selection. Dpo4 is also captured in the crystal translocating two template bases to the active site at once, suggesting a possible mechanism for bypassing thymine dimers.
引用
收藏
页码:91 / 102
页数:12
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