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J. Biol. Chem., Vol. 269, Issue 16, 11845-11851, Apr, 1994
M Gorospe and C Baglioni
Labeled transcripts of interleukin-1 alpha (IL-1 alpha) cDNA were rapidly
degraded in incubations with rabbit reticulocyte lysate (RRL). In contrast,
a transcript of superoxide dismutase cDNA was stable in control
incubations. A transcript of the 3'-untranslated region (UTR) of IL-1 alpha
was rapidly degraded while that of the 5'-UTR and coding region was stable.
This degradative activity was present in the post- ribosomal supernatant.
Degradation of the 3'-UTR transcript was inhibited by the addition of a
large excess of an 80-base RNA containing four AUUUA repeats, but not by
the same RNA without such repeats. This suggested that AUUUA motifs were
responsible for the instability of the 3'-UTR transcript. The 80-base RNA
did not act as a competitive substrate for a nuclease since it was not
degraded. Partial transcripts of IL-1 alpha 3'-UTR were incubated with RRL
to localize instability determinants. Transcripts containing at least three
clustered AUUUA motifs were rapidly degraded, while transcripts containing
four scattered AUUUA motifs were stable. To study the mechanism of RNA
degradation, the RRL was passed through an affinity column that retained
AUUUA-binding proteins. The flow-through or the fraction eluted from such a
column were inactive, but the two fractions together degraded the 3'-UTR
transcript. This indicated that proteins bound by the affinity column did
not have nuclease activity but targeted this RNA for degradation.
Degradation of unstable interleukin-1 alpha mRNA in a rabbit reticulocyte cell-free system. Localization of an instability determinant to a cluster of AUUUA motifs
Department of Biological Sciences, State University of New York, Albany 12222.
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