SRP RNA remodeling by SRP68 explains its role in protein translocation
The signal recognition particle (SRP) is central to membrane protein targeting; SRP RNA is essential for SRP assembly, elongation arrest, and activation of SRP guanosine triphosphatases. In eukaryotes, SRP function relies on the SRP68-SRP72 heterodimer. We present the crystal structures of the RNA-b...
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| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
04 Apr 2014
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| In: |
Science
Year: 2014, Jahrgang: 344, Heft: 6179, Pages: 101-104 |
| ISSN: | 1095-9203 |
| DOI: | 10.1126/science.1249094 |
| Online-Zugang: | Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1126/science.1249094 Verlag, lizenzpflichtig, Volltext: https://science.sciencemag.org/content/344/6179/101 
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| Verfasserangaben: | Jan Timo Grotwinkel, Klemens Wild, Bernd Segnitz, Irmgard Sinning |
| Zusammenfassung: | The signal recognition particle (SRP) is central to membrane protein targeting; SRP RNA is essential for SRP assembly, elongation arrest, and activation of SRP guanosine triphosphatases. In eukaryotes, SRP function relies on the SRP68-SRP72 heterodimer. We present the crystal structures of the RNA-binding domain of SRP68 (SRP68-RBD) alone and in complex with SRP RNA and SRP19. |
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| Beschreibung: | Gesehen am 18.09.2020 |
| Beschreibung: | Online Resource |
| ISSN: | 1095-9203 |
| DOI: | 10.1126/science.1249094 |