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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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Bibliographic Details
Main Authors: Grotwinkel, Jan Timo (Author) , Wild, Klemens (Author) , Segnitz, Bernd (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: 04 Apr 2014
In: Science
Year: 2014, Volume: 344, Issue: 6179, Pages: 101-104
ISSN:1095-9203
DOI:10.1126/science.1249094
Online Access: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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Author Notes:Jan Timo Grotwinkel, Klemens Wild, Bernd Segnitz, Irmgard Sinning
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Summary: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.
Item Description:Gesehen am 18.09.2020
Physical Description:Online Resource
ISSN:1095-9203
DOI:10.1126/science.1249094

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