期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 22, 期 11, 页码 906-913出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3103
关键词
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资金
- National Natural Science Foundation of China [31170677, 31422016]
- Ministry of Science and Technology of China [2013CB910404]
- Swedish Research Council [2010-2619, 2011-6088, 2014-4423, 2008-6593]
- Knut and Alice Wallenberg Foundation [KAW 2011.0081]
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 coil 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.
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