The RNA helicase HrpA rescues collided ribosomes in E. coli. Campbell et al

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Campbell, Annabelle

Description

Although many antibiotics inhibit bacterial ribosomes, loss of known factors that rescue stalled ribosomes does not lead to robust antibiotic sensitivity in E. coli, suggesting the existence of additional mechanisms. Here, we show that the RNA helicase HrpA rescues stalled ribosomes in E. coli. Acting selectively on ribosomes that have collided, HrpA uses ATP hydrolysis to split stalled ribosomes into subunits. Cryo-EM structures reveal how HrpA simultaneously binds to two collided ribosomes, explaining its selectivity, and how its helicase module engages downstream mRNA, such that by exerting a pulling force on the mRNA, it would destabilize the stalled ribosome. These studies show that ribosome splitting is a conserved mechanism that allows proteobacteria to tolerate ribosome-targeting antibiotics.

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Metrics

Dataset Index

0.4

FAIR Score

65%

Citations

0

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0

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Publication Details

DOI

Publisher

Mendeley Data

License

Creative Commons Attribution 4.0 International

Assigned Domain

Subfield

Molecular Biology

Field

Biochemistry, Genetics and Molecular Biology

Domain

Life Sciences

Confidence Score

46%

Source

Scholar Data Model

Keywords

BiochemistryMolecular BiologyCryo-Electron MicroscopyRibosomeTranslation (Protein Synthesis)Escherichia coliHelicaseAntibiotic Resistance

Normalization Factors

FT

53.85

CTw

1.00

MTw

1.00