| Online-Ressource |
Verfasst von: | Li, Weihan [VerfasserIn]  |
| Crotty, Kelly [VerfasserIn]  |
| Garrido Ruiz, Diego [VerfasserIn]  |
| Voorhies, Mark [VerfasserIn]  |
| Rivera, Carlos [VerfasserIn]  |
| Sil, Anita [VerfasserIn]  |
| Mullins, R Dyche [VerfasserIn]  |
| Jacobson, Matthew P [VerfasserIn]  |
| Peschek, Jirka [VerfasserIn]  |
| Walter, Peter [VerfasserIn]  |
Titel: | Protomer alignment modulates specificity of RNA substrate recognition by Ire1 |
Verf.angabe: | Weihan Li, Kelly Crotty, Diego Garrido Ruiz, Mark Voorhies, Carlos Rivera, Anita Sil, R Dyche Mullins, Matthew P Jacobson, Jirka Peschek, Peter Walter |
E-Jahr: | 2021 |
Jahr: | 27 April 2021 |
Umfang: | 20 S. |
Teil: | volume:10 |
| year:2021 |
| elocationid:e67425 |
| pages:1-20 |
| extent:20 |
Fussnoten: | Gesehen am 22.07.2021 |
Titel Quelle: | Enthalten in: eLife |
Ort Quelle: | Cambridge : eLife Sciences Publications, 2012 |
Jahr Quelle: | 2021 |
Band/Heft Quelle: | 10(2021), Artikel-ID e67425, Seite 1-20 |
ISSN Quelle: | 2050-084X |
Abstract: | The unfolded protein response (UPR) maintains protein folding homeostasis in the endoplasmic reticulum (ER). In metazoan cells, the Ire1 branch of the UPR initiates two functional outputs—non-conventional mRNA splicing and selective mRNA decay (RIDD). By contrast, Ire1 orthologs from Saccharomyces cerevisiae and Schizosaccharomyces pombe are specialized for only splicing or RIDD, respectively. Previously, we showed that the functional specialization lies in Ire1’s RNase activity, which is either stringently splice-site specific or promiscuous (Li et al., 2018). Here, we developed an assay that reports on Ire1’s RNase promiscuity. We found that conversion of two amino acids within the RNase domain of S. cerevisiae Ire1 to their S. pombe counterparts rendered it promiscuous. Using biochemical assays and computational modeling, we show that the mutations rewired a pair of salt bridges at Ire1 RNase domain’s dimer interface, changing its protomer alignment. Thus, Ire1 protomer alignment affects its substrates specificity. |
DOI: | doi:10.7554/eLife.67425 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.7554/eLife.67425 |
| DOI: https://doi.org/10.7554/eLife.67425 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | enzymatic substrate specificity |
| Ire1 |
| RNA biology |
| unfolded protein response |
K10plus-PPN: | 1764185943 |
Verknüpfungen: | → Zeitschrift |
Protomer alignment modulates specificity of RNA substrate recognition by Ire1 / Li, Weihan [VerfasserIn]; 27 April 2021 (Online-Ressource)