DNA聚合酶α与校对模型。
DNA polymerase alpha and models for proofreading.
作者信息
Abbotts J, Loeb L A
出版信息
Nucleic Acids Res. 1985 Jan 11;13(1):261-74. doi: 10.1093/nar/13.1.261.
Abstract
Using a modified system to measure fidelity at an amber site in phi X174, we have employed DNA polymerase alpha to test different mechanisms for proofreading. DNA polymerase alpha does not exhibit the characteristics of "kinetic proofreading" seen with procaryotic polymerases. Polymerase alpha shows no evidence for a "next nucleotide" effect, and added deoxynucleoside monophosphates do not alter fidelity. Pyrophosphate, which increases error rates with a procaryotic polymerase, appears to weakly improve polymerase alpha fidelity. DNA polymerase alpha does exhibit a dramatic increase in error rate in the presence of a deoxycytidine thiotriphosphate (dCTP alpha S), but this enhanced mutagenesis also occurs under conditions where kinetic proofreading should be otherwise defeated. This particular effect with dCTP alpha S appears specific for DNA polymerase alpha and is not seen with the other polymerases tested.
摘要
我们使用一种经过改良的系统来测量φX174中琥珀密码子位点的保真度，利用DNA聚合酶α来测试不同的校对机制。DNA聚合酶α不具备原核生物聚合酶所具有的“动力学校对”特征。聚合酶α没有显示出“下一个核苷酸”效应的证据，添加的脱氧核苷单磷酸也不会改变保真度。焦磷酸会增加原核生物聚合酶的错误率，但似乎能微弱地提高聚合酶α的保真度。在存在脱氧胞苷三磷酸硫代物（dCTPαS）的情况下，DNA聚合酶α的错误率会显著增加，但这种增强的诱变作用也会在动力学校对本应失效的条件下出现。dCTPαS的这种特殊效应似乎对DNA聚合酶α具有特异性，在所测试的其他聚合酶中未观察到。
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本文引用的文献
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