Identification of homologous pairing and strand-exchange activity from a human tumor cell line based on Z-DNA affinity chromatography.

Identification of homologous pairing and strand-exchange activity from a human tumor cell line based on Z-DNA affinity chromatography.
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基于 Z-DNA 亲和层析鉴定人类肿瘤细胞系的同源配对和链交换活性。

DOI:
10.1073/pnas.85.1.36
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发表时间:
1988
影响因子:
11.1
通讯作者:
Rich,A
Rich,A
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Fishel,RA;Detmer,K;Rich,A

文献摘要

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催化双链线性DNA和单链环状DNA的ATP依赖性同源配对和链交换的酶活性已从人白血病T淋巴母细胞细胞系中纯化数千倍。在Z-DNA柱基质上对核蛋白进行层析后鉴定活性。该反应显示从供体双链体线性底物将互补单链转移到病毒环状单链受体,从5'末端开始,并以3'方向进行(5 '-3')。链转移反应的产物,其特征在于通过电子显微镜。一个74 kDa的蛋白被确定为主要的ATP结合肽的活性链转移酶馏分。本报告中描述的蛋白质制剂与Z-DNA的结合比与B-DNA的结合更强。
An enzymatic activity that catalyzes ATP-dependent homologous pairing and strand exchange of duplex linear DNA and single-stranded circular DNA has been purified several thousand-fold from a human leukemic T-lymphoblast cell line. The activity was identified after chromatography of nuclear proteins on a Z-DNA column matrix. The reaction was shown to transfer the complementary single strand from a donor duplex linear substrate to a viral circular single-stranded acceptor beginning at the 5' end and proceeding in the 3' direction (5'----3'). Products of the strand-transfer reaction were characterized by electron microscopy. A 74-kDa protein was identified as the major ATP-binding peptide in active strand transferase fractions. The protein preparation described in this report binds more strongly to Z-DNA than to B-DNA.