HflX is a Ribosome-splitting Factor Rescuing Stalled Ribosomes Under Stress Conditions

Overview

Journal Nat Struct Mol Biol

Specialties Cell Biology
Molecular Biology

Date 2015 Oct 13

PMID 26458047

Citations 58

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

Affiliations

Soon will be listed here.

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 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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