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Background  Camptothecin is a plant alkaloid that specifically binds topoisomerase I, inhibiting its activity and inducing double stranded breaks in DNA and activating the cell responses to DNA damage.    Results  Maize cultured cells were incubated in the presence of different concentrations of camptothecin. Camptothecin inhibits cultured cell growth, induces genomic DNA degradation, and induces a 32 kDa Ca 2+ /Mg 2+ -dependent nuclease activity. This nuclease, we called CaMNUC32, is inhibited by Zn 2+  and by acid pH, it is mainly localized in the nucleus and it cleaves single- and double-stranded DNA, with a higher activity against single-stranded DNA. Two-dimensional electrophoresis combined with mass spectrometry suggests that CaMNUC32 is a member of the type I S1/P1 nuclease family. This type of nucleases are usually Zn 2+ -dependent but our results support previous indications that S1-type nucleases have a wide variety of enzyme activities, including Ca 2+ /Mg 2+ -dependent.    Conclusions  We have identified and characterized CaMNUC32, a 32 kDa Ca 2+ /Mg 2+ -dependent nuclease of the S1/P1 family induced by the topoisomerase I inhibitor camptothecin in maize cultured cells.

Identification of a type I Ca2+/Mg2+-dependent endonuclease induced in maize cells exposed to camptothecin