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TitleStructure of the hibernating 100S ribosome reveals the basis for 70S dimerization.
Journal, issue, pagesEMBO J, Vol. 36, Issue 14, Page 2061-2072, Year 2017
Publish dateJul 14, 2017
AuthorsBertrand Beckert / Maha Abdelshahid / Heinrich Schäfer / Wieland Steinchen / Stefan Arenz / Otto Berninghausen / Roland Beckmann / Gert Bange / Kürşad Turgay / Daniel N Wilson /
PubMed AbstractUnder stress conditions, such as nutrient deprivation, bacteria enter into a hibernation stage, which is characterized by the appearance of 100S ribosomal particles. In , dimerization of 70S ...Under stress conditions, such as nutrient deprivation, bacteria enter into a hibernation stage, which is characterized by the appearance of 100S ribosomal particles. In , dimerization of 70S ribosomes into 100S requires the action of the ribosome modulation factor (RMF) and the hibernation-promoting factor (HPF). Most other bacteria lack RMF and instead contain a long form HPF (LHPF), which is necessary and sufficient for 100S formation. While some structural information exists as to how RMF and HPF mediate formation of 100S (100S), structural insight into 100S formation by LHPF has so far been lacking. Here we present a cryo-EM structure of the hibernating 100S (100S), revealing that the C-terminal domain (CTD) of the LHPF occupies a site on the 30S platform distinct from RMF Moreover, unlike RMF, the HPF-CTD is directly involved in forming the dimer interface, thereby illustrating the divergent mechanisms by which 100S formation is mediated in the majority of bacteria that contain LHPF, compared to some γ-proteobacteria, such as .
External linksEMBO J / PubMed:28468753 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 6.2 Å
Structure data

3656

5njt

EMDB-3656, PDB-5njt:
Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization.
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-3664:
Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization.
Method: EM (single particle) / Resolution: 6.2 Å

Source
  • bacillus subtilis subsp. subtilis str. 168 (bacteria)
  • Bacillus subtilis (bacteria)
KeywordsTRANSLATION / 100S / Bacillus subtilis / cryo-EM / Hibernation / HPF / RMF / rRNA / YvyD

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