Kilpatrick M W, Wei C F, Gray H B, Wells R D
Nucleic Acids Res. 1983 Jun 11;11(11):3811-22. doi: 10.1093/nar/11.11.3811.
The BAL 31 nuclease, an extracellular nuclease from A. espejiana, specifically recognizes and cleaves the salt induced conformational junction between B and Z-DNA. Short segments of (dC-dG) left-handed Z-helix, comprising approximately 1% of the total DNA, are specifically detected within two different recombinant plasmids. The BAL 31 enzyme is highly resistant to inactivation by the presence of high concentrations of a variety of electrolytes that stabilize left-handed helices, is active at physiological pH, and can be used to probe both linear and circular DNAs. Additionally, the nuclease cleaves left-handed (dC-dG)n only very poorly, if at all. Thus, the BAL 31 nuclease can be utilized as a probe for helical junctions and consequently for segments of left-handed DNA that might exist within predominantly right-handed naturally occurring genomes.
BAL 31核酸酶是一种来自埃氏艾美球虫的细胞外核酸酶,它能特异性识别并切割由盐诱导形成的B-DNA与Z-DNA之间的构象连接。在两种不同的重组质粒中,特别检测到了占总DNA约1%的左手Z-螺旋(dC-dG)短片段。BAL 31酶对多种能稳定左手螺旋的高浓度电解质的存在具有高度抗性,在生理pH值下具有活性,可用于探测线性和环状DNA。此外,该核酸酶切割左手(dC-dG)n的能力很差,甚至根本无法切割。因此,BAL 31核酸酶可作为螺旋连接的探针,进而用于探测可能存在于以右手螺旋为主的天然基因组中的左手DNA片段。