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J. Biol. Chem., Vol. 276, Issue 26, 23922-23928, June 29, 2001
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From the Eukaryotic initiation factor (eIF) 4B interacts
with several components of the initiation pathway and is targeted for
cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B
interacts with the poly(A)-binding protein and that a region consisting
of the N-terminal 80 amino acids of eIF4B is both necessary and
sufficient for such binding. This interaction is lost when eIF4B is
cleaved by caspase-3, which removes the N-terminal 45 amino acids.
Similarly, the association of eIF4B with the poly(A)-binding protein
in vivo is reduced when cells are induced to undergo
apoptosis. Cleavage of the poly(A)-binding protein itself, using human
rhinovirus 3C protease, also eliminates the interaction with eIF4B.
Thus, disruption of the association between mammalian eIF4B and
the poly(A)-binding protein can occur during both apoptosis and
picornaviral infection and is likely to contribute to the inhibition of
translation observed under these conditions.
Disruption of the Interaction of Mammalian Protein
Synthesis Eukaryotic Initiation Factor 4B with the
Poly(A)-binding Protein by Caspase- and Viral Protease-mediated
Cleavages*
§,
, and**
Department of Biochemistry and Immunology,
Cellular and Molecular Sciences Group, St. George's Hospital Medical
School, Cranmer Terrace, London SW17 0RE, United Kingdom and the
¶ Department of Biochemistry, School of Biological Sciences,
University of Sussex, Brighton BN1 9QG, United Kingdom
*
Research in our laboratories is supported by grants from the
Wellcome Trust (Grants 040800, 058915, 057494, 045619, and 056778), the
Leukemia Research Fund, the Cancer Prevention Research Trust, and
Glaxo-Wellcome.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.
Senior Research Fellow of the Wellcome Trust.
**
To whom correspondence should be addressed. Tel.: 44-020-8725-5762;
Fax: 44-020-8725-2992; E-mail: M.Clemens@sghms.ac.uk.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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