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Vol. 12, Issue 11, 3644-3657, November 2001
Department of Biological Chemistry, The University of Michigan
Medical School, Ann Arbor, Michigan 48109-0606
Under stressful conditions organisms adjust the synthesis,
processing, and trafficking of molecules to allow survival from and
recovery after stress. In baker's yeast Saccharomyces
cerevisiae, the cellular production of ribosomes is tightly
matched with environmental conditions and nutrient availability through
coordinate transcriptional regulation of genes involved in ribosome
biogenesis. On the basis of stress-responsive gene expression and
functional studies, we have identified a novel, evolutionarily
conserved gene, EMG1, that has similar stress-responsive
gene expression patterns as ribosomal protein genes and is required for
the biogenesis of the 40S ribosomal subunit. The Emg1 protein is
distributed throughout the cell; however, its nuclear localization
depends on physical interaction with a newly characterized nucleolar
protein, Nop14. Yeast depleted of Nop14 or harboring a
temperature-sensitive allele of emg1 have selectively
reduced levels of the 20S pre-rRNA and mature18S rRNA and diminished
cellular levels of the 40S ribosomal subunit. Neither Emg1 nor Nop14
contain any characterized functional motifs; however, isolation and
functional analyses of mammalian orthologues of Emg1 and Nop14 suggest
that these proteins are functionally conserved among eukaryotes. We
conclude that Emg1 and Nop14 are novel proteins whose interaction is
required for the maturation of the 18S rRNA and for 40S ribosome production.
Corresponding author. E-mail address:
dthiele{at}umich.edu.
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