8RD8

Cryo-EM structure of P. urativorans 70S ribosome in complex with hibernation factors Balon and RaiA (structure 1).

これはPDB形式変換不可エントリーです。

8RD8 の概要

• エントリーDOI: 10.2210/pdb8rd8/pdb
• EMDBエントリー: 19067
• 分子名称: Methyl-accepting chemotaxis protein, Large ribosomal subunit protein uL5, 5S rRNA, ... (56 entities in total)
• 機能のキーワード: ribosome, hibernation factor, dormancy, balon
• 由来する生物種: Psychrobacter urativorans; 詳細
• タンパク質・核酸の鎖数: 55
• 化学式量合計: 2269520.59

構造登録者

Helena-Bueno, K.,Rybak, M.Y.,Gagnon, M.G.,Hill, C.H.,Melnikov, S.V. (登録日: 2023-12-07, 公開日: 2024-02-21, 最終更新日: 2024-03-13)

主引用文献

Helena-Bueno, K.,Rybak, M.Y.,Ekemezie, C.L.,Sullivan, R.,Brown, C.R.,Dingwall, C.,Basle, A.,Schneider, C.,Connolly, J.P.R.,Blaza, J.N.,Csorgo, B.,Moynihan, P.J.,Gagnon, M.G.,Hill, C.H.,Melnikov, S.V.
A new family of bacterial ribosome hibernation factors.
Nature, 626:1125-1132, 2024

PubMed Abstract: To conserve energy during starvation and stress, many organisms use hibernation factor proteins to inhibit protein synthesis and protect their ribosomes from damage. In bacteria, two families of hibernation factors have been described, but the low conservation of these proteins and the huge diversity of species, habitats and environmental stressors have confounded their discovery. Here, by combining cryogenic electron microscopy, genetics and biochemistry, we identify Balon, a new hibernation factor in the cold-adapted bacterium Psychrobacter urativorans. We show that Balon is a distant homologue of the archaeo-eukaryotic translation factor aeRF1 and is found in 20% of representative bacteria. During cold shock or stationary phase, Balon occupies the ribosomal A site in both vacant and actively translating ribosomes in complex with EF-Tu, highlighting an unexpected role for EF-Tu in the cellular stress response. Unlike typical A-site substrates, Balon binds to ribosomes in an mRNA-independent manner, initiating a new mode of ribosome hibernation that can commence while ribosomes are still engaged in protein synthesis. Our work suggests that Balon-EF-Tu-regulated ribosome hibernation is a ubiquitous bacterial stress-response mechanism, and we demonstrate that putative Balon homologues in Mycobacteria bind to ribosomes in a similar fashion. This finding calls for a revision of the current model of ribosome hibernation inferred from common model organisms and holds numerous implications for how we understand and study ribosome hibernation.

PubMed: 38355796
DOI: 10.1038/s41586-024-07041-8

実験手法

ELECTRON MICROSCOPY (2.62 Å)