An RNasin-resistant ribonuclease selective for interleukin 2 mRNA.

Abstract:

: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 beta-globin mRNA. Pancreatic RNase, by contrast, does not show a significant preference for IL2 mRNA. Neither 5' capping, nor polyadenylation of the substrate mRNAs affects their degradation by the IL2-selective 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 beta-globin mRNA does not.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Hua J,Garner R,Paetkau V

doi

10.1093/nar/21.1.155

subject

Has Abstract

pub_date

1993-01-11 00:00:00

pages

155-62

issue

1

eissn

0305-1048

issn

1362-4962

journal_volume

21

pub_type

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