Use of 2-aminopurine fluorescence to study the role of the beta hairpin in the proofreading pathway catalyzed by the phage T4 and RB69 DNA polymerases.
Use of 2-aminopurine fluorescence to study the role of the beta hairpin in the proofreading pathway catalyzed by the phage T4 and RB69 DNA polymerases.
复制标题
使用 2-氨基嘌呤荧光研究 β 发夹在噬菌体 T4 和 RB69 DNA 聚合酶催化的校对途径中的作用。
DOI:
10.1021/bi800211f
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发表时间:
2008
期刊:
影响因子:
2.9
通讯作者:
Reha-Krantz,LindaJ
中科院分区:
文献类型:
--
作者:
Subuddhi,Usharani;Hogg,Matthew;Reha-Krantz,LindaJ
For DNA polymerases to proofread a misincorporated nucleotide, the terminal 3−4 nucleotides of the primer strand must be separated from the template strand before being bound in the exonuclease active center. Genetic and biochemical studies of the bacteriophage T4 DNA polymerase revealed that a prominent β-hairpin structure in the exonuclease domain is needed to efficiently form the strand-separated exonuclease complexes. We present here further mutational analysis of the loop region of the T4 DNA polymerase β-hairpin structure, which provides additional evidence that residues in the loop, namely, Y254 and G255, are important for DNA replication fidelity. The mechanism of strand separation was probed inin vitroreactions using the fluorescence of the base analogue 2-aminopurine (2AP) and mutant RB69 DNA polymerases that have modifications to the β hairpin, to the exonuclease active site, or to both. We propose from these studies that the β hairpin in the exonuclease domain of the T4 and RB69 DNA polymerases functions to facilitate strand separation, but residues in the exonuclease active center are required to capture the 3′ end of the primer strand following strand separation.