结构减法作为一种研究限制性内切酶作用机制的方法。
Structure subtraction as an approach to investigation of the mechanism of restriction enzyme action.
作者信息
Zinoviev V V, Gorbunov J A, Baclanov M M, Popov S G, Malygin E G
出版信息
FEBS Lett. 1983 Apr 18;154(2):282-4. doi: 10.1016/0014-5793(83)80166-5.
Endonuclease BamHI cleaves the phosphodiester bonds between the guanine residues within the duplex DNA sequence G decreases GATCC. The substrate characteristics of oligonucleotides, containing some defects in the sequence recognized by endonuclease (nick, absence of some internucleotide phosphate or nucleotide, partially single-stranded form of the recognition site) were investigated. The results suggest that the specificity of synthetic oligonucleotide cleavage is strongly dependent on the ribosophosphate backbone intactness inside the recognition site. BamHI was found not to hydrolyse the phosphodiester bonds outside the double helix. Also BamHI forms a productive complex with the non-symmetrical substrate, having half the recognition sites, of a single strand.
核酸内切酶BamHI可切割双链DNA序列G↓GATCC中鸟嘌呤残基之间的磷酸二酯键。研究了在核酸内切酶识别序列中存在某些缺陷（切口、某些核苷酸间磷酸或核苷酸缺失、识别位点部分单链形式）的寡核苷酸的底物特性。结果表明，合成寡核苷酸切割的特异性强烈依赖于识别位点内核糖磷酸主链的完整性。发现BamHI不会水解双螺旋外的磷酸二酯键。此外，BamHI可与具有单链一半识别位点的非对称底物形成有效复合物。
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