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Title | HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 22, Issue 11, Page 906-913, Year 2015 |
Publish date | Oct 12, 2015 |
Authors | 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 Abstract | 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. |
External links | Nat Struct Mol Biol / PubMed:26458047 |
Methods | EM (single particle) |
Resolution | 4.5 Å |
Structure data | |
Chemicals | ChemComp-GNP: ChemComp-MG: |
Source |
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Keywords | RIBOSOME / RIBOSOME RESCUE |