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

verfasst von
Bertrand Beckert, Maha Abdelshahid, Heinrich Schäfer, Wieland Steinchen, Stefan Arenz, Otto Berninghausen, Roland Beckmann, Gert Bange, Kürşad Turgay, Daniel N. Wilson
Abstract

Under stress conditions, such as nutrient deprivation, bacteria enter into a hibernation stage, which is characterized by the appearance of 100S ribosomal particles. In Escherichia coli, 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 E. coli 100S (Ec100S), structural insight into 100S formation by LHPF has so far been lacking. Here we present a cryo-EM structure of the Bacillus subtilis hibernating 100S (Bs100S), revealing that the C-terminal domain (CTD) of the LHPF occupies a site on the 30S platform distinct from RMF. Moreover, unlike RMF, the BsHPF-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 E. coli.

Organisationseinheit(en)
Naturwissenschaftliche Fakultät
Institut für Mikrobiologie
Externe Organisation(en)
Ludwig-Maximilians-Universität München (LMU)
Philipps-Universität Marburg
Universität Hamburg
Typ
Artikel
Journal
EMBO Journal
Band
36
Seiten
2061-2072
Anzahl der Seiten
12
ISSN
0261-4189
Publikationsdatum
14.07.2017
Publikationsstatus
Veröffentlicht
Peer-reviewed
Ja
ASJC Scopus Sachgebiete
Neurowissenschaften (insg.), Molekularbiologie, Biochemie, Genetik und Molekularbiologie (insg.), Immunologie und Mikrobiologie (insg.)
Elektronische Version(en)
https://doi.org/10.15252/embj.201696189 (Zugang: Offen)