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Nucleic Acids Research, 1983, Vol. 11, No. 11 3811-3822
© 1983

MOLECULAR BIOLOGY

BAL 31 nuclease as a probe in concentrated salt for the B-Z DNA junction

Michael W. Kilpatrick*, Chik-Fong Wei+, Horace B. Gray, Jr+ and Robert D. Wells*

*Department of Biochemistry, University of Alabama in Birmingham, Schools of Medicine and Dentistry Birmingham, AL 35294, USA +Department of Biochemical and Biophysical Sciences, University of Houston Houston, TX 77004, USA

Received February 21, 1983. Accepted May 29, 1983.

The BAL 31 nuclease, an extracellular nuclease from A. eapejiana, specifically recognizes and cleaves the salt induced conformational junction between B and Z–DNA. Short segments of (dC–dG) left-handed Z–helix, comprising {small tilde}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.


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