Functional analysis of the mammalian RNA ligase for IRE1 in the unfolded protein response
| Autor: | Juthakorn Poothong, Randal J. Kaufman, Witoon Tirasophon |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
X-Box Binding Protein 1 Saccharomyces cerevisiae Proteins RNA Splicing Biophysics Saccharomyces cerevisiae Biology Protein Serine-Threonine Kinases Endoplasmic Reticulum Biochemistry Ligases 03 medical and health sciences Exon Escherichia coli Animals Humans RNA Messenger Molecular Biology Research Articles RNA ligase chemistry.chemical_classification Mammals DNA ligase Membrane Glycoproteins Endoplasmic reticulum Intron Rlg1p RNA Cell Biology Exons human IRE1α/XBP1 Endoplasmic Reticulum Stress human RtcB Introns archease DNA-Binding Proteins Repressor Proteins 030104 developmental biology Basic-Leucine Zipper Transcription Factors chemistry rlg1-100 RNA splicing Unfolded protein response Unfolded Protein Response Research Article Signal Transduction |
| Zdroj: | Bioscience Reports |
| ISSN: | 1573-4935 0144-8463 |
| Popis: | The unfolded protein response (UPR) is a conserved signalling pathway activated on the accumulation of unfolded proteins within the endoplasmic reticulum (ER), termed ER stress. Upon ER stress, HAC1/XBP1 undergoes exon/intron-specific excision by inositol requiring enzyme 1 (IRE1) to remove an intron and liberate the 5′ and 3′ exons. In yeast, the 5′ and 3′ HAC1 exons are subsequently ligated by tRNA ligase (Rlg1p), whereas XBP1 ligation in mammalian cells is catalysed by a recently identified ligase, RtcB. In the present study, RNA ligase activity of the human RtcB (hRtcB) involved in the unconventional splicing of XBP1/HAC1 mRNA was explored in an rlg1-100 mutant yeast strain. Distinct from Escherichia coli RtcB and Rlg1p, expression of hRtcB alone inefficiently complemented HAC1/XBP1 splicing and the hRtcB cofactor (archease) was required to promote enzymatic activity of hRtcB to catalyse RNA ligation. |
| Databáze: | OpenAIRE |
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