Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling
Daniel Sohmen,
Shinobu Chiba,
Naomi Shimokawa-Chiba,
C. Axel Innis,
Otto Berninghausen,
Roland Beckmann,
Koreaki Ito and
Daniel N. Wilson ()
Additional contact information
Daniel Sohmen: University of Munich
Shinobu Chiba: Faculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku
Naomi Shimokawa-Chiba: Faculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku
C. Axel Innis: Institut Européen de Chimie et Biologie, Université de Bordeaux
Otto Berninghausen: University of Munich
Roland Beckmann: University of Munich
Koreaki Ito: Faculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku
Daniel N. Wilson: University of Munich
Nature Communications, 2015, vol. 6, issue 1, 1-10
Abstract:
Abstract Ribosomal stalling is used to regulate gene expression and can occur in a species-specific manner. Stalling during translation of the MifM leader peptide regulates expression of the downstream membrane protein biogenesis factor YidC2 (YqjG) in Bacillus subtilis, but not in Escherichia coli. In the absence of structures of Gram-positive bacterial ribosomes, a molecular basis for species-specific stalling has remained unclear. Here we present the structure of a Gram-positive B. subtilis MifM-stalled 70S ribosome at 3.5–3.9 Å, revealing a network of interactions between MifM and the ribosomal tunnel, which stabilize a non-productive conformation of the PTC that prevents aminoacyl-tRNA accommodation and thereby induces translational arrest. Complementary genetic analyses identify a single amino acid within ribosomal protein L22 that dictates the species specificity of the stalling event. Such insights expand our understanding of how the synergism between the ribosome and the nascent chain is utilized to modulate the translatome in a species-specific manner.
Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (4)
Downloads: (external link)
https://www.nature.com/articles/ncomms7941 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7941
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/ncomms7941
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().