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Genes and Development
Vol. 11, No. 19,
pp. 2557-2568,
October 1, 1997
Department of Molecular Biophysics and Biochemistry, Howard Hughes
Medical Institute, Yale University School of Medicine, Boyer Center for
Molecular Medicine, New Haven, Connecticut 06520 USA
AU-rich elements (AREs, usually containing repeated copies of
AUUUA), when present in the 3
-untranslated regions (UTRs) of many
mammalian mRNAs, confer instability on their host RNA molecules. The
viral small nuclear RNA (snRNA) Herpesvirus saimiri U RNA 1 (HSUR 1) also contains an AUUUA-rich sequence. Here, we report that
this ARE induces rapid degradation of HSUR 1 itself and of other snRNAs
including HSUR 2 and cellular U1. Mutational analyses of the viral ARE
establish that sequence requirements for mRNA and snRNA decay are the
same, suggesting a similar mechanism. Moreover, the in vivo degradation
activity of mutant AREs correlates with their in vitro binding to the
HuR protein, implicated previously as a component of the mRNA
degradation machinery. Our results suggest that ARE-mediated
instability can be uncoupled from both ongoing translation and
deadenylation of the target RNA.
[Key Words: ARE; HSUR 1; RNA degradation; HuR; Herpesvirus saimiri]
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