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J. Biol. Chem., Vol. 277, Issue 6, 4147-4151, February 8, 2002
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From the Whitney Laboratory, University of Florida, St. Augustine,
Florida 32080
Coordinate regulation of the ribosomal
protein genes is entrusted to a number of signal transduction pathways
that can abruptly induce or silence the ribosomal genes. We have
uncovered a cellular model system, which selectively induces the
ribosomal protein S25 gene in hepatoma cells that are stressed by
nutrient deprivation. Our results indicate that p53 along with two
other identified proteins, MTF-1 and La, post-transcriptionally
regulate the synthesis of the S25 protein by controlling the nuclear
export of the stress-induced S25 mRNA. This system is unique in
that the nuclear-retained S25 mRNA is exported to the cytosol
only upon replenishment or alternatively after prolonged starvation to
participate in a p53-mediated apoptotic sequence of events. This
p53-dependent survival or death pathway involves a
previously unreported protein relationship among these three actors,
one of which, MTF-1, has not yet been shown to have RNA-binding characteristics.
Ribosomal Protein S25 mRNA Partners with MTF-1 and La to
Provide a p53-mediated Mechanism for Survival or Death*
*
This work was supported in part by the National
Institutes of Health Grant DK49644.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 should be addressed: The
Whitney Laboratory, University of Florida, 9505 Ocean Shore Blvd., St.
Augustine, FL 32080. Tel.: 904-461-4031; Fax: 904-461-4008; E-mail:
laine@whitney.ufl.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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