Abstract
Three different genome-scale screens indicate that the HAC1 mRNA is the only substrate for the Ire1 nuclease in yeast.
Highlights
The unfolded protein response (UPR) allows intracellular feedback regulation that adjusts the protein-folding capacity of the endoplasmic reticulum (ER) according to need
Recombinant Ire1* expressed and purified from E. coli is incubated with poly(A)+ RNA isolated from wild-type S. cerevisiae to cleave endogenous HAC1 mRNA and other potential RNA substrates of Ire1p
Cleaved RNA (lacking the poly(A) tail) is separated from uncleaved RNA as the unbound, poly(A)- fraction from an oligo(dT) column and used to prepare fluorescent probe by reverse transcription followed by polymerase chain reaction (PCR) amplification in the presence of Cy3-dTTP
Summary
The unfolded protein response (UPR) allows intracellular feedback regulation that adjusts the protein-folding capacity of the endoplasmic reticulum (ER) according to need. The unfolded protein response (UPR) regulates the proteinfolding and secretory capacity of eukaryotic cells by monitoring conditions within the endoplasmic reticulum (ER) and regulating a downstream gene-expression program (reviewed in [1,2,3]). About 5% of the genome is under the transcriptional control of the UPR [4,5] Induction of this vast set of genes is thought to lead to a restructuring of the secretory. The UPR is initiated when the amino-terminal portion of the serine/threonine ER-transmembrane kinase Ire detects unfolded proteins within the ER lumen [6,7]. Oligomerization, in turn, results in trans-autophosphorylation of the cytosolic kinase domain, providing the means by which the signal is transmitted across the ER membrane
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