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Originally published In Press as doi:10.1074/jbc.M007236200 on October 19, 2000
J. Biol. Chem., Vol. 276, Issue 3, 2122-2131, January 19, 2001
Plant Initiation Factor 3 Subunit Composition Resembles Mammalian
Initiation Factor 3 and Has a Novel Subunit*
Elizabeth A.
Burks,
Paula P.
Bezerra,
Hahn
Le ,
Daniel R.
Gallie , and
Karen S.
Browning§
From the Department of Chemistry and Biochemistry and the Institute
for Cellular and Molecular Biology, University of Texas, Austin, Texas
78712 and the Department of Biochemistry, University of
California, Riverside, California 92521
Eukaryotic initiation factor 3 (eIF3) is a
multisubunit complex that is required for binding of mRNA to 40 S
ribosomal subunits, stabilization of ternary complex binding to 40 S
subunits, and dissociation of 40 and 60 S subunits. These functions and
the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. Recently, the subunits of
mammalian and Saccharomyces cerevisiae eIF3 were
identified, and substantial differences in the subunit composition of
mammalian and S. cerevisiae were observed. Mammalian eIF3
consists of 11 nonidentical subunits, whereas S. cerevisiae
eIF3 consists of up to eight nonidentical subunits. Only five of the
subunits of mammalian and S. cerevisiae are shared in
common, and these five subunits comprise a "core" complex in
S. cerevisiae. eIF3 from wheat consists of at least 10 subunits, but their relationship to either the mammalian or S. cerevisiae eIF3 subunits is unknown. Peptide sequences derived
from purified wheat eIF3 subunits were used to correlate each subunit
with mammalian and/or S. cerevisiae subunits. The peptide
sequences were also used to identify Arabidopsis thaliana
cDNAs for each of the eIF3 subunits. We report seven new cDNAs
for A. thaliana eIF3 subunits. A. thaliana eIF3
was purified and characterized to confirm that the subunit composition and activity of wheat and A. thaliana eIF3 were similar. We
report that plant eIF3 closely resembles the subunit composition of
mammalian eIF3, having 10 out of 11 subunits in common. Further, we
find a novel subunit in the plant eIF3 complex not present in either mammalian or S. cerevisiae eIF3. These results suggest that
plant and mammalian eIF3 evolved similarly, whereas S. cerevisiae has diverged.
*
This work was supported by National Science Foundation Grant
MCB 980873, Department of Energy Grant DE-FG03-97ER20283, Welch Foundation Grant F-1339 (to K. S. B.), and United States Department of Agriculture Grant 00-35301-9086 (to D. R. G.).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) AF291711, AF285834, AF291714, AF285832, AF291712, AF285833,
AF285835, and AF291713.
§
To whom correspondence should be addressed. Tel.: 512-471-4562;
Fax: 512-471-8696: E-mail: kbrowning@mail.utexas.edu.
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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