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J. Biol. Chem., Vol. 276, Issue 12, 8695-8704, March 23, 2001
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From the Department of Molecular Genetics and Microbiology,
University of Medicine and Dentistry of New Jersey, Robert Wood Johnson
Medical School, Piscataway, New Jersey 08854
In mammals, A+U-rich elements (AREs) are potent
cis-acting determinants of rapid cytoplasmic mRNA
turnover. Recognition of these sequences by AUF1 is associated with
acceleration of mRNA decay, likely involving recruitment or
assembly of multi-subunit trans-acting complexes.
Previously, we demonstrated that AUF1 deletion mutants formed tetramers
on U-rich RNA substrates by sequential addition of protein dimers
(Wilson, G. M., Sun, Y., Lu, H., and Brewer, G. (1999)
J. Biol. Chem. 274, 33374-33381). Here, we show that
binding of the full-length p37 isoform of AUF1 to these RNAs proceeds
via a similar mechanism, allowing delineation of
equilibrium binding constants for both stages of tetramer assembly. However, association of AUF1 with the ARE from tumor necrosis factor
(TNF
Folding of A+U-rich RNA Elements Modulates AUF1 Binding
POTENTIAL ROLES IN REGULATION OF mRNA TURNOVER*
,
) mRNA was significantly inhibited by magnesium ions. Further fluorescence and hydrodynamic experiments indicated that Mg2+ induced or stabilized a conformational change in the
TNF ARE. Based on the solution of parameters describing both the
protein-RNA and Mg2+-RNA equilibria, we present a dynamic,
global equilibrium binding model describing the relationship between
Mg2+ and AUF1 binding to the TNF ARE. These studies
provide the first evidence that some AREs may adopt higher order RNA
structures that regulate their interaction with
trans-acting factors and indicate that mRNA structural
remodeling has the potential to modulate the turnover rates of some
ARE-containing mRNAs.
*
This work was funded by Grant R01 CA 52443 from the National
Institutes of Health and a grant from the Arthritis Foundation (to
G. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed: Dept. of Molecular
Genetics and Microbiology, University of Medicine and Dentistry of New
Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854. Tel.: 732-235-3379; Fax: 732-235-5223; E-mail:
wilsongm@umdnj.edu.
§
To whom correspondence may be addressed: Dept. of Molecular
Genetics and Microbiology, University of Medicine and Dentistry of New
Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854. Tel.:
732-235-3473; Fax: 732-235-5223; E-mail: brewerga@umdnj.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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