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Nucleic Acids Research, 1990, Vol. 18, No. 6 1407-1413
© 1990

MOLECULAR BIOLOGY

Purification and characterization of the in vitro activity of I-Sce I, a novel and highly specific endonuclease encoded by a group I intron

Claude Monteilhet+, Arnaud Perrin, Agnès Thierry, Laurence Colleaux and Bernard Dujon*

Unité de Génétique moléculaire des Levures, Institut Pasteur 25 rue du Docteur Roux, F-75724 Pans-Cedex 15, France

*To whom correspondence should be addressed

Received December 29, 1989. Revised January 23, 1990. Accepted January 23, 1990.

Group I intron encoded proteins represent a novel class of site specific double strand endonucleases. The endonuclease activity of this class of proteins has been first demonstrated in vivo for I-Sce I which is encoded by a mitochondrial intron of Saccharomyces cerevisiae. Assays using crude cell extracts have shown that I-Sce I can be used in vitro as a restriction endonuclease potentially useful for recombinant DNA technology owing to its large recognition sequence (18 nucleotides). We report here the purification and the first detailed analysis of the in vitro activity and properties of I-Sce I.

+ Permanent address Centre de Génélique moléculaure du CNRS, F-91198 Gif sur Yvette, France


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