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-Structure paper
タイトル | Structure of the hibernating 100S ribosome reveals the basis for 70S dimerization. |
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ジャーナル・号・ページ | EMBO J, Vol. 36, Issue 14, Page 2061-2072, Year 2017 |
掲載日 | 2017年7月14日 |
著者 | Bertrand Beckert / Maha Abdelshahid / Heinrich Schäfer / Wieland Steinchen / Stefan Arenz / Otto Berninghausen / Roland Beckmann / Gert Bange / Kürşad Turgay / Daniel N Wilson / |
PubMed 要旨 | 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 ...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 . |
リンク | EMBO J / PubMed:28468753 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.8 - 6.2 Å |
構造データ | EMDB-3656, PDB-5njt: EMDB-3664: |
由来 |
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キーワード | TRANSLATION / 100S / Bacillus subtilis / cryo-EM / Hibernation / HPF / RMF / rRNA / YvyD |