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J Biol Chem, Vol. 273, Issue 49, 32870-32877, December 4, 1998

A Ribosomal Protein Is Required for Translational Regulation of GCN4 mRNA
EVIDENCE FOR INVOLVEMENT OF THE RIBOSOME IN eIF2 RECYCLING

Peter P. Mueller^§¶, Patrick Grueter, Alan G. Hinnebusch^§, and Hans Trachsel

From the  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

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.

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