Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization-Reference-Cited by-同舟云学术

Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization

Published:2017-05-03 Issue:14 Volume:36 Page:2061-2072
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:EMBO J

Author:

Beckert Bertrand¹,Abdelshahid Maha¹,Schäfer Heinrich²,Steinchen Wieland³,Arenz Stefan¹,Berninghausen Otto¹,Beckmann Roland¹,Bange Gert³^ORCID,Turgay Kürşad²^ORCID,Wilson Daniel N¹⁴^ORCID

Affiliation:

1. Gene Center Department for Biochemistry and Center for integrated Protein Science Munich (CiPSM) University of Munich Munich Germany

2. Naturwissenschaftliche Fakultät Institut für Mikrobiologie Leibniz Universität Hannover Hannover Germany

3. LOEWE Center for Synthetic Microbiology and Faculty of Chemistry Philipps University Marburg Marburg Germany

4. Institute for Biochemistry and Molecular Biology University of Hamburg Hamburg Germany

Funder

Deutsche Forschungsgemeinschaft

Publisher

EMBO

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.201696189

Reference60 articles.

1. PHENIX: a comprehensive Python-based system for macromolecular structure solution

2. The ribosome-associated inhibitor A reduces translation errors

3. Modulation of mRNA Stability Participates in Stationary-Phase-Specific Expression of Ribosome Modulation Factor

4. Ribosome dimerization is essential for the efficient regrowth of Bacillus subtilis

5. Ribosome hibernation factor promotesStaphylococcalsurvival and differentially represses translation

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