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Nucleic Acids Research, 1994, Vol. 22, No. 8 1456-1462
© 1994

MOLECULAR BIOLOGY

Purification of a calcium dependent ribonuclease from Xenopus laevis

Christopher W. Seidel+ and Lawrence J. Peck*

Sinsheimer Laboratories, University of California Santa Cruz, CA 95064, USA

*To whom correspondence should be addressed

Received December 15, 1993. Revised March 11, 1994. Accepted March 11, 1994.

We have purified a Ca2+ dependent ribonuclease from the oocytes of Xenopus lea vis. Two properties of this ribonuclease set it apart from other known nucleases. First, Ca2+ was required for ribonuclease activity, and Mg2+ would not substitute. Second, the enzyme specifically degraded RNA and digestion of double or single stranded DNA was not observed. Ca2+ dependent ribonuclease activity of the purified 36-kDa protein was directly observed after renaturatlon of the protein following electrophoresls in an SDS-Laemmli gel. In addition, the enzyme was shown to have endoribonuclease activity at numerous sites. The Ca2+ dependence suggests that the ribonuclease activity may be modulated by changes in the level of Intracellular Ca2+ and thereby provide a direct link to signal transductlon systems.

+ Present address: Department of Molecular and Cellular Biology, University of California, Berkeley, CA 94720, USA


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