Isolation and characterization of high affinity aptamers against DNA polymerase iota.
Isolation and characterization of high affinity aptamers against DNA polymerase iota.
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针对 DNA 聚合酶 iota 的高亲和力适体的分离和表征。
DOI：
10.1089/nat.2011.0324
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发表时间：
2012
影响因子：
4
通讯作者：
L. Gening
中科院分区：
文献类型：
--
作者：
A. V. Lakhin;A. A. Kazakov;A. Makarova;Y. Pavlov;A. Efremova;S. Shram;V. Z. Tarantul;L. Gening
人类dna聚合酶（Pol ι）是一种极容易出错的酶，其保真度取决于模板的序列背景。利用指数富集（SELEX）方法对配体进行体外系统进化，我们获得了一个与人类Pol ι具有高亲和力的寡核苷酸，命名为适体IKL5。我们用均相制备的方法测定了它的解离常数，并预测了它的二级结构。适体IKL5特异性抑制纯化酶Pol ι的DNA聚合酶活性，但不抑制人DNA聚合酶β和kappa的DNA聚合酶活性。在肿瘤细胞系SKOV-3的细胞提取物中，IKL5也能抑制Pol ι易出错的dna聚合酶活性。适配体IKL5可用于研究Pol ι的生物学作用，并可作为抑制恶性细胞中该酶活性增加的潜在药物。
Human DNA-polymerase iota (Pol ι) is an extremely error-prone enzyme and the fidelity depends on the sequence context of the template. Using the in vitro systematic evolution of ligands by exponential enrichment (SELEX) procedure, we obtained an oligoribonucleotide with a high affinity to human Pol ι, named aptamer IKL5. We determined its dissociation constant with homogenous preparation of Pol ι and predicted its putative secondary structure. The aptamer IKL5 specifically inhibits DNA-polymerase activity of the purified enzyme Pol ι, but did not inhibit the DNA-polymerase activities of human DNA polymerases beta and kappa. IKL5 suppressed the error-prone DNA-polymerase activity of Pol ι also in cellular extracts of the tumor cell line SKOV-3. The aptamer IKL5 is useful for studies of the biological role of Pol ι and as a potential drug to suppress the increase of the activity of this enzyme in malignant cells.
影响因子：
10.5
作者：
A. Tissier;J. McDonald;E. G. Frank;R. Woodgate
通讯作者：
A. Tissier;J. McDonald;E. G. Frank;R. Woodgate
影响因子：
4
作者：
Plosky, BS;Woodgate, R
通讯作者：
Woodgate, R
通过 RNA 单链构象多态性 (rSSCP) 筛选突变：与 DNA-SSCP 的比较。
影响因子：
14.9
作者：
Sarkar,G;Yoon,HS;Sommer,SS
通讯作者：
Sommer,SS