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J Biol Chem, Vol. 275, Issue 5, 3377-3381, February 4, 2000
From the Department of Biological Chemistry and the Howard Hughes
Medical Institute, University of Michigan Medical Center, Ann Arbor,
Michigan 48109-0650
Accumulation of unfolded proteins in the
endoplasmic reticulum (ER) activates signaling pathways to induce
transcription of a number of genes encoding ER protein chaperones
and-folding catalysts. In Saccharomyces cerevisiae this
transcriptional induction is mediated by an increase in the synthesis
of the transcription factor Hac1p. The transmembrane receptor
Ire1p/Ern1p containing a Ser/Thr protein kinase and endoribonuclease
activity transmits the unfolded protein response (UPR) from the ER to
the nucleus. Activation of Ire1p kinase induces its endoribonuclease
activity to cleave unspliced HAC1 mRNA and generate
exon fragments that are subsequently ligated by tRNA ligase
(RLG1). Whereas unspliced HAC1 mRNA is
poorly translated, spliced HAC1 mRNA is efficiently translated. Subunits of the yeast transcriptional co-activator complex
SAGA also play a role in the UPR. Deletion of GCN5,
ADA2, or ADA3 reduces, and deletion of
ADA5 completely abolishes, the UPR. Although
HAC1 mRNA requires only Ire1p and Rlg1p in
vitro, we demonstrate that ADA5 is required for the
IRE1/RLG1-dependent splicing reaction of
HAC1 mRNA in vivo. In addition, Ada5p
interacts with Ire1p. These results suggest that subcomponents of
transcriptional co-activator complexes may be involved in RNA
processing events.
The Transcriptional Co-activator ADA5 Is Required
for HAC1 mRNA Processing in Vivo*
,
*
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.
Present address: Dept. of Internal Medicine, Div. of Nephrology,
The University of Michigan Medical Center, 1150 W. Medical Center Dr.,
Ann Arbor, MI 48109.
§
To whom correspondence should be addressed: Dept. of Biological
Chemistry and the Howard Hughes Medical Institute, The University of
Michigan Medical Center, 1150 W. Medical Center Dr., Ann Arbor, MI
48109-0650. Tel.: 734-763-9037; Fax: 734-763-9323; E-mail: kaufmanr@umich.edu.
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