Nucleic Acids Research, Vol 26, Issue 4 1063-1069, Copyright © 1998 by Oxford University Press
K Mizuta, R Tsujii, JR Warner and M Nishiyama
We have previously shown that a functional secretory pathway is essential
for continued ribosome synthesis in Saccharomyces cerevisiae. When a
temperature-sensitive mutant defective in the secretory pathway is
transferred to the non-permissive temperature, transcription of both rRNA
genes and ribosomal protein genes is nearly abolished. In order to define
the cis -acting element(s) of ribosomal protein genes sensitive to a defect
in the secretory pathway, we have constructed a series of fusion genes
containing the CYH2 promoter region, with various deletions, fused to lacZ.
Each fusion gene for which transcription is detected is subject to the
repression. Rap1p is the transcriptional activator for most ribosomal
protein genes, as well as having an important role in silencing in the
vicinity of telomeres and at the silent mating-type loci. To assess its
role in the repression of transcription by the defect in the secretory
pathway, we have introduced rap1 mutations. The replacement of wild-type
Rap1p by Rap1p truncated at the C-terminal region caused substantial
attenuation of the repression. Furthermore, we have demonstrated that the
Rap1p- truncation affects the repression of TCM1 , encoding ribosomal
protein L3, which has no Rap1p-binding site in its upstream regulatory
region. These results suggest that the repression of transcription of
ribosomal protein genes by a secretory defect is mediated through Rap1p,
but does not require a Rap1p-binding site within the UAS.
ARTICLES
The C-terminal silencing domain of Rap1p is essential for the repression of ribosomal protein genes in response to a defect in the secretory pathway
Department of Biochemistry and Biophysics, Research Institute for Radiation Biology and Medicine, Hiroshima University, Hiroshima 734, Japan. kmizuta@ipc.hiroshima-u.ac.jp
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