Abstract
The dynamin superfamily of large GTPases comprises specialized members that catalyze fusion and fission of biological membranes. While fission-specific proteins such as dynamin work as homo-oligomeric complexes, many fusion catalysts such as mitofusins or bacterial dynamin-like proteins (DLPs) act as hetero-oligomers. However, so far it was unclear how these hetero-oligomeric DLPs assemble and how they function in membrane remodeling. The group of Harry Low report now on the structure of a DLP pair from Campylobacter jejuni, allowing detailed insight into the assembly mechanism and membrane tethering activity.
Highlights
The dynamin superfamily of large GTPases comprises specialized members that catalyze fusion and fission of biological membranes
Bacterial dynamin-like proteins (DLPs) Most bacterial DLPs are encoded in an operon with two adjacent genes, suggesting that they act as heterotypic complexes to eukaryotic MFN and OPA1
Similar to the structure of LeoA, a bacterial DLP encoded in enterotoxigenic Escherichia coli[7], the four-helix bundle of C. jejuni DLP2 lacks a distinct hinge region between neck and trunk
Summary
The dynamin superfamily of large GTPases comprises specialized members that catalyze fusion and fission of biological membranes. Structural data suggest that DFS proteins catalyzing membrane fusion and fission can be separated by their domain architecture[1]. Several DLPs involved in membrane fusion act as hetero-oligomeric complexes.
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