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Global profiling of SRP interaction with nascent polypeptides

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Here, the selection of substrates by the protein-RNA complex known as the signal recognition particle (SRP) is investigated in the bacterium Escherichia coli, revealing that the SRP has a strong preference for hydrophobic transmembrane domains of inner membrane proteins.

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Bibliographic Details
Main Authors: Schibich, Daniela (Author) , Gloge, Felix (Author) , Pöhner, Ina (Author) , Björkholm, Patrik (Author) , Wade, Rebecca C. (Author) , Heijne, Gunnar von (Author) , Bukau, Bernd (Author) , Kramer, Günter (Author)
Format: Article (Journal)
Language:English
Published: 3 August 2016
In: Nature
Year: 2016, Volume: 536, Issue: 7615, Pages: 219-223
ISSN:1476-4687
DOI:10.1038/nature19070
Online Access:Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1038/nature19070
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nature19070
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Author Notes:Daniela Schibich, Felix Gloge, Ina Pöhner, Patrik Björkholm, Rebecca C. Wade, Gunnar von Heijne, Bernd Bukau & Günter Kramer
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Summary:Here, the selection of substrates by the protein-RNA complex known as the signal recognition particle (SRP) is investigated in the bacterium Escherichia coli, revealing that the SRP has a strong preference for hydrophobic transmembrane domains of inner membrane proteins.
Item Description:Das PDF enthält zusätzlich einen Anhang von 11 Seiten
Gesehen am 13.05.2020
Physical Description:Online Resource
ISSN:1476-4687
DOI:10.1038/nature19070

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