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Engineering ER-stress dependent non-conventional mRNA splicing.
Li, Weihan; Okreglak, Voytek; Peschek, Jirka; Kimmig, Philipp; Zubradt, Meghan; Weissman, Jonathan S; Walter, Peter.
Afiliación
  • Li W; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
  • Okreglak V; Howard Hughes Medical Institute, San Francisco, United States.
  • Peschek J; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
  • Kimmig P; Howard Hughes Medical Institute, San Francisco, United States.
  • Zubradt M; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
  • Weissman JS; Howard Hughes Medical Institute, San Francisco, United States.
  • Walter P; Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
Elife ; 72018 07 09.
Article en En | MEDLINE | ID: mdl-29985129
The endoplasmic reticulum (ER) protein folding capacity is balanced with the protein folding burden to prevent accumulation of un- or misfolded proteins. The ER membrane-resident kinase/RNase Ire1 maintains ER protein homeostasis through two fundamentally distinct processes. First, Ire1 can initiate a transcriptional response through a non-conventional mRNA splicing reaction to increase the ER folding capacity. Second, Ire1 can decrease the ER folding burden through selective mRNA decay. In Saccharomyces cerevisiae and Schizosaccharomyces pombe, the two Ire1 functions have been evolutionarily separated. Here, we show that the respective Ire1 orthologs have become specialized for their functional outputs by divergence of their RNase specificities. In addition, RNA structural features separate the splicing substrates from the decay substrates. Using these insights, we engineered an S. pombe Ire1 cleavage substrate into a splicing substrate, which confers S. pombe with both Ire1 functional outputs.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Schizosaccharomyces / Ingeniería Genética / Empalme del ARN / Estrés del Retículo Endoplásmico Idioma: En Revista: Elife Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Schizosaccharomyces / Ingeniería Genética / Empalme del ARN / Estrés del Retículo Endoplásmico Idioma: En Revista: Elife Año: 2018 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido