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Nucleic Acids Research, 1993, Vol. 21, No. 1 155-162
© 1993

ENZYMOLOGY

An RNasin-resistant ribonuclease selective for interleukin 2 mRNA

Jaling Hua, Rosemary Garner and Verner Paetkau*

Department of Biochemistry, Medical Sciences Building, University of Alberta Edmonton, Alberta T6G 2H7, Canada

*To whom correspondence should be addressed

Received July 8, 1992. Accepted December 2, 1992.

Interleukin 2 (IL2) mRNA has a short half-life in the cytoplasm of T lymphocytes, relative to most mRNA. We have discovered a candidate ribonuclease to account for the rapid turnover of IL2 mRNA in the cytosol of the human T lymphocyte cell line Jurkat. In partially purified form, this RNase is about 7 times as active on IL2 as on ß-globin mRNA. Pancreatic RNase, by contrast, does not show a significant preference for IL2 mRNA. Neither 5' capping, nor polyadenylatlon of the substrate mRNAs affects their degradation by the IL2-selectlve mRNase, whose activity is optimal in 0.5 mM Mg++ and 100 mM potassium acetate. The mRNase behaves like a protein of molecular weight 60–70,000 on gel chromatography, and is unusual in that it is insensitive to placental RNase inhibitor (RNasin). The mRNase cleaves IL2 mRNA at a small number of sites in the coding region, and IL2 mRNA containing only the coding region and 36 nucleotides of the 3'-noncoding region competes efficiently with full-length IL2 mRNA for the mRNase, whereas ß-globin mRNA does not.


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