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Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization
Author(s) -
Beckert Bertrand,
Abdelshahid Maha,
Schäfer Heinrich,
Steinchen Wieland,
Arenz Stefan,
Berninghausen Otto,
Beckmann Roland,
Bange Gert,
Turgay Kürşad,
Wilson Daniel N
Publication year - 2017
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.201696189
Subject(s) - biology , bacillus subtilis , ribosome , microbiology and biotechnology , genetics , bacteria , rna , gene
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 ( Ec 100S), 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 ( Bs 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 Bs 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 E. coli .