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Originally published In Press as doi:10.1074/jbc.M006721200 on October 11, 2000
J. Biol. Chem., Vol. 276, Issue 1, 334-340, January 5, 2001
Arabidopsis eIF3e (INT-6) Associates with Both eIF3c
and the COP9 Signalosome Subunit CSN7*
Avital
Yahalom ,
Tae-Houn
Kim§,
Eitan
Winter ,
Baruch
Karniol ,
Albrecht G.
von Arnim§, and
Daniel A.
Chamovitz ¶
From the Department of Plant Sciences, Tel
Aviv University, Tel Aviv 69978, Israel and § Department
of Botany, the University of Tennessee,
Knoxville, Tennessee 37996-1100
The Arabidopsis COP9 signalosome is a
multisubunit repressor of photomorphogenesis that is conserved among
eukaryotes. This complex may have a general role in development. As a
step in dissecting the biochemical mode of action of the COP9
signalosome, we determined the sequence of proteins that copurify with
this complex. Here we describe the association between components of
the COP9 signalosome (CSN1, CSN7, and CSN8) and two subunits of
eukaryotic translation initiation factor 3 (eIF3), eIF3e (p48, known
also as INT-6) and eIF3c (p105). To obtain a biochemical marker for
Arabidopsis eIF3, we cloned the Arabidopsis
ortholog of the eIF3 subunit eIF3b (PRT1). eIF3e coimmunoprecipitated
with CSN7, and eIF3c coimmunoprecipitated with eIF3e, eIF3b, CSN8, and
CSN1. eIF3e directly interacted with CSN7 and eIF3c. However, eIF3e and
eIF3b cofractionated by gel filtration chromatography in a complex that
was larger than the COP9 signalosome. Whereas eIF3, as detected through
eIF3b, localized solely to the cytoplasm, eIF3e, like CSN7, was also
found in the nucleus. This suggests that eIF3e and eIF3c are probably
components of multiple complexes and that eIF3e and eIF3c associate
with subunits of the COP9 signalosome, even though they are not
components of the COP9 signalosome core complex. This interaction may
allow for translational control by the COP9 signalosome.
*
This work was supported by Grant 96-00258 from the United
States-Israel Binational Science Foundation (to D. A. C. and
A. G. v. A.).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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF255679 and AF255680.
¶
To whom correspondence should be addressed. Tel.:
972-3-6408989; Fax: 972-3-6409380; E-mail: chamd@post.tau.ac.il.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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