Imperial College London

Dr Sophie Helaine

Faculty of MedicineDepartment of Medicine

Senior Lecturer
 
 
 
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Contact

 

+44 (0)20 7594 3976s.helaine

 
 
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Location

 

2.20Flowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Cheverton:2016:10.1016/j.molcel.2016.05.002,
author = {Cheverton, AM and Gollan, B and Przydacz, M and Wong, CT and Mylona, A and Hare, SA and Helaine, S},
doi = {10.1016/j.molcel.2016.05.002},
journal = {Molecular cell},
pages = {86--96},
title = {A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNA.},
url = {http://dx.doi.org/10.1016/j.molcel.2016.05.002},
volume = {63},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The recalcitrance of many bacterial infections to antibiotic treatment is thought to be due to the presence of persisters that are non-growing, antibiotic-insensitive cells. Eventually, persisters resume growth, accounting for relapses of infection. Salmonella is an important pathogen that causes disease through its ability to survive inside macrophages. After macrophage phagocytosis, a significant proportion of the Salmonella population forms non-growing persisters through the action of toxin-antitoxin modules. Here we reveal that one such toxin, TacT, is an acetyltransferase that blocks the primary amine group of amino acids on charged tRNA molecules, thereby inhibiting translation and promoting persister formation. Furthermore, we report the crystal structure of TacT and note unique structural features, including two positively charged surface patches that are essential for toxicity. Finally, we identify a detoxifying mechanism in Salmonella wherein peptidyl-tRNA hydrolase counteracts TacT-dependent growth arrest, explaining how bacterial persisters can resume growth.
AU - Cheverton,AM
AU - Gollan,B
AU - Przydacz,M
AU - Wong,CT
AU - Mylona,A
AU - Hare,SA
AU - Helaine,S
DO - 10.1016/j.molcel.2016.05.002
EP - 96
PY - 2016///
SN - 1097-2765
SP - 86
TI - A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNA.
T2 - Molecular cell
UR - http://dx.doi.org/10.1016/j.molcel.2016.05.002
UR - http://hdl.handle.net/10044/1/33362
VL - 63
ER -