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-Structure paper
| タイトル | HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions. |
|---|---|
| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 22, Issue 11, Page 906-913, Year 2015 |
| 掲載日 | 2015年10月12日 |
著者 | Yanqing Zhang / Chandra Sekhar Mandava / Wei Cao / Xiaojing Li / Dejiu Zhang / Ningning Li / Yixiao Zhang / Xiaoxiao Zhang / Yan Qin / Kaixia Mi / Jianlin Lei / Suparna Sanyal / Ning Gao / ![]() |
| PubMed 要旨 | Adverse cellular conditions often lead to nonproductive translational stalling and arrest of ribosomes on mRNAs. Here, we used fast kinetics and cryo-EM to characterize Escherichia coli HflX, a ...Adverse cellular conditions often lead to nonproductive translational stalling and arrest of ribosomes on mRNAs. Here, we used fast kinetics and cryo-EM to characterize Escherichia coli HflX, a GTPase with unknown function. Our data reveal that HflX is a heat shock-induced ribosome-splitting factor capable of dissociating vacant as well as mRNA-associated ribosomes with deacylated tRNA in the peptidyl site. Structural data demonstrate that the N-terminal effector domain of HflX binds to the peptidyl transferase center in a strikingly similar manner as that of the class I release factors and induces dramatic conformational changes in central intersubunit bridges, thus promoting subunit dissociation. Accordingly, loss of HflX results in an increase in stalled ribosomes upon heat shock. These results suggest a primary role of HflX in rescuing translationally arrested ribosomes under stress conditions. |
リンク | Nat Struct Mol Biol / PubMed:26458047 |
| 手法 | EM (単粒子) |
| 解像度 | 4.5 Å |
| 構造データ | |
| 化合物 | ![]() ChemComp-GNP: ![]() ChemComp-MG: |
| 由来 |
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キーワード | RIBOSOME / RIBOSOME RESCUE |
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