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J Biol Chem, Vol. 273, Issue 49, 32870-32877, December 4, 1998
From the In amino acid-starved yeast cells, inhibition of
the guanine nucleotide exchange factor eIF2B by phosphorylated
translation initiation factor 2 results in increased translation of
GCN4 mRNA. We isolated a suppressor of a mutant eIF2B.
The suppressor prevents efficient GCN4 mRNA translation
due to inactivation of the small ribosomal subunit protein Rps31 and
results in low amounts of mutant 40 S ribosomal subunits. Deletion of
one of two genes encoding ribosomal protein Rps17 also reduces the
amounts of 40 S subunits but does not suppress eIF2B mutations or
prevent efficient GCN4 translation. Our findings show that
Rps31-deficient ribosomes are altered in a way that decreases the eIF2B
requirement and that the small ribosomal subunit mediates the effects
of low eIF2B activity on cell viability and translational regulation in
response to eIF2 phosphorylation.
A Ribosomal Protein Is Required for Translational Regulation
of GCN4 mRNA
EVIDENCE FOR INVOLVEMENT OF THE RIBOSOME IN eIF2 RECYCLING
§¶,
,
Institute of Biochemistry and Molecular
Biology, University of Berne, CH-3012 Berne, Switzerland, the
§ Laboratory of Eukaryotic Gene Regulation, NICHHD, National
Institutes of Health, Bethesda, Maryland 20892, and ¶ RDIF/GBF,
National Research Institute for Biotechnology, Mascheroder Weg 1, D-38124 Braunschweig, Germany
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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