Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 2061-2072 |
| Seitenumfang | 12 |
| Fachzeitschrift | EMBO Journal |
| Jahrgang | 36 |
| Ausgabenummer | 14 |
| Publikationsstatus | Veröffentlicht - 14 Juli 2017 |
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.
ASJC Scopus Sachgebiete
- Neurowissenschaften (insg.)
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Immunologie und Mikrobiologie (insg.)
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in: EMBO Journal, Jahrgang 36, Nr. 14, 14.07.2017, S. 2061-2072.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization
AU - Beckert, Bertrand
AU - Abdelshahid, Maha
AU - Schäfer, Heinrich
AU - Steinchen, Wieland
AU - Arenz, Stefan
AU - Berninghausen, Otto
AU - Beckmann, Roland
AU - Bange, Gert
AU - Turgay, Kürşad
AU - Wilson, Daniel N.
N1 - Funding information: We thank Heidimarie Sieber, Charlotte Ungewickell, and Susanne Rieder for expert technical assistance; Uwe Linne (Marburg) for mass spectrometry support; and Beckmann-Coulter GmbH (Krefeld, Germany) for kindly providing the DelsaMax CORE. This research was supported by grants from the Deutsche Forschungsgemeinschaft (SPP-1879 to K.T., G.B., and D.N.W.).
PY - 2017/7/14
Y1 - 2017/7/14
N2 - 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.
AB - 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.
KW - cryo-EM
KW - hibernation
KW - HPF
KW - RMF
KW - translation
UR - http://www.scopus.com/inward/record.url?scp=85018979980&partnerID=8YFLogxK
U2 - 10.15252/embj.201696189
DO - 10.15252/embj.201696189
M3 - Article
C2 - 28468753
AN - SCOPUS:85018979980
VL - 36
SP - 2061
EP - 2072
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 14
ER -