Structural basis for membrane tethering by a bacterial dynamin-like pair.

Autor:	Liu J; Department of Life Sciences, Imperial College, London, SW7 2AZ, UK., Noel JK; Max Delbrück Center for Molecular Medicine, Kristallographie, Robert-Rössle-Strasse 10, Berlin, 13125, Germany., Low HH; Department of Life Sciences, Imperial College, London, SW7 2AZ, UK. h.low@imperial.ac.uk.
Jazyk:	angličtina
Zdroj:	Nature communications [Nat Commun] 2018 Aug 21; Vol. 9 (1), pp. 3345. Date of Electronic Publication: 2018 Aug 21.
DOI:	10.1038/s41467-018-05523-8
Abstrakt:	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.
Databáze:	MEDLINE
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