A 5' to 3' exonuclease functionally interacts with calf DNA polymerase epsilon.
A 5' to 3' exonuclease functionally interacts with calf DNA polymerase epsilon.
复制标题
5 至 3 核酸外切酶与小牛 DNA 聚合酶 epsilon 发生功能性相互作用。
DOI：
10.1073/pnas.89.20.9377
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发表时间：
1992
影响因子：
11.1
通讯作者：
Bambara,RA
中科院分区：
文献类型：
--
作者：
Siegal,G;Turchi,JJ;Myers,TW;Bambara,RA
Analysis of fractions containing purified DNA polymerase epsilon from calf thymus has revealed the presence of a 5' to 3' exonuclease activity that is specific for a single strand of duplex DNA. This activity is capable of degrading a 3'-labeled oligonucleotide hybridized to M13mp18 DNA. When a second oligonucleotide primer is annealed 3 bases upstream, degradation of the downstream primer is strictly dependent on DNA synthesis from the upstream primer. Replacement of the downstream primer by an oligoribonucleotide of identical sequence results in a similar pattern of exonucleolytic activity. The activity has been highly purified and found to cosediment in glycerol gradients with a peptide of 56 kDa as judged by SDS/PAGE analysis. Effects of calf DNA polymerase alpha and delta on exonuclease activity are also observed but with differences in the pattern of products.
