3'至5'核酸外切酶活性与噬菌体029 DNA聚合酶相关。

A 3' to 5' exonuclease activity is associated with phage 029 DNA polymerase.

作者信息

Watabe K, Leusch M S, Ito J

出版信息

Biochem Biophys Res Commun. 1984 Sep 28;123(3):1019-26. doi: 10.1016/s0006-291x(84)80235-1.

DOI:10.1016/s0006-291x(84)80235-1

Abstract

Bacteriophage 029 produces its own DNA polymerase which is encoded by gene 2 [Watabe, K. and Ito, J. (1983) Nucleic Acid Res. 11, 8333]. This 029 DNA polymerase has been purified by phospho-cellulose, DEAE-cellulose, double-stranded DNA cellulose chromatography and glycerol gradient centrifugation. An exonuclease activity associated with the DNA polymerase was found through all the steps of the purification. This nuclease preferably degrades single-stranded DNA from the 3' to the 5' terminus direction, suggesting that the enzyme plays a role for proofreading during DNA replication. While DNA polymerase activity isolated from cells infected with temperature sensitive mutant of gene 2 is thermolabile, the nuclease activity is not significantly reduced at the restrictive temperature.

摘要

噬菌体029产生自身的DNA聚合酶，该酶由基因2编码[渡边，K.和伊藤，J.（1983年）《核酸研究》11，8333]。这种029 DNA聚合酶已通过磷酸纤维素、二乙氨基乙基纤维素、双链DNA纤维素色谱法和甘油梯度离心法进行了纯化。在纯化的所有步骤中都发现了与DNA聚合酶相关的核酸外切酶活性。这种核酸酶优先从3'到5'末端方向降解单链DNA，这表明该酶在DNA复制过程中起校对作用。虽然从感染了基因2温度敏感突变体的细胞中分离出的DNA聚合酶活性是热不稳定的，但在限制温度下核酸酶活性并未显著降低。

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