Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions

Beckert, Bertrand and Kedrov, Alexej and Sohmen, Daniel and Kempf, Georg and Wild, Klemens and Sinning, Irmgard and Stahlberg, Henning and Wilson, Daniel N. and Beckmann, Roland. (2015) Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions. Nature structural & molecular biology, 22 (10). pp. 767-773.

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Official URL: http://edoc.unibas.ch/40163/

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The signal recognition particle (SRP) recognizes signal sequences of nascent polypeptides and targets ribosome-nascent chain complexes to membrane translocation sites. In eukaryotes, translating ribosomes are slowed down by the Alu domain of SRP to allow efficient targeting. In prokaryotes, however, little is known about the structure and function of Alu domain-containing SRPs. Here, we report a complete molecular model of SRP from the Gram-positive bacterium Bacillus subtilis, based on cryo-EM. The SRP comprises two subunits, 6S RNA and SRP54 or Ffh, and it facilitates elongation slowdown similarly to its eukaryotic counterpart. However, protein contacts with the small ribosomal subunit observed for the mammalian Alu domain are substituted in bacteria by RNA-RNA interactions of 6S RNA with the α-sarcin-ricin loop and helices H43 and H44 of 23S rRNA. Our findings provide a structural basis for cotranslational targeting and RNA-driven elongation arrest in prokaryotes.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Stahlberg)
UniBasel Contributors:Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publ. Group
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:30 Jun 2016 11:00
Deposited On:14 Jun 2016 06:36

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