Imperial College London
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DrHarryLow

Faculty of Medicine, Department of Infectious Disease

Senior Wellcome Trust Fellow and Proleptic Reader
 
 
 
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Contact

 

+44 (0)20 7594 3064h.low

 
 
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Location

 

260Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Liu:2018:10.1038/s41467-018-05523-8,
author = {Liu, J and Noel, J and Low, HH},
doi = {10.1038/s41467-018-05523-8},
journal = {Nature Communications},
pages = {1--12},
title = {Structural basis for membrane tethering ­by a bacterial dynamin-like pair},
url = {http://dx.doi.org/10.1038/s41467-018-05523-8},
volume = {9},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Dynamin-like proteins (DLPs) are large GTPases that restructure membrane. DLPs such as the mitofusins form heterotypic oligomers between isoform pairs that bridge and fuse opposing membranes. In bacteria, heterotypic oligomerisation may also be important for membrane remodelling as most DLP genes are paired within operons. How DLPs tether opposing membranes is unknown. Here we show the crystal structure of a DLP heterotypic pair from the pathogen Campylobacter jejuni. A 2:2 stoichiometric tetramer is observed where heterodimers, conjoined by a random coil linker, assemble back-to-back to form a tripartite DLP chain with extreme flexibility. In vitro, tetramerisation triggers GTPase activity and induces lipid binding. Liposomes are readily tethered and form tubes at high tetramer concentration. Our results provide a direct mechanism for the long-range binding and bridging of opposing membranes by a bacterial DLP pair. They also provide broad mechanistic and structural insights that are relevant to other heterotypic DLP complexes.
AU  - Liu,J
AU  - Noel,J
AU  - Low,HH
DO  - 10.1038/s41467-018-05523-8
EP  - 12
PY  - 2018///
SN  - 2041-1723
SP  - 1
TI  - Structural basis for membrane tethering ­by a bacterial dynamin-like pair
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-018-05523-8
UR  - https://www.nature.com/articles/s41467-018-05523-8
UR  - http://hdl.handle.net/10044/1/62598
VL  - 9
ER  -
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