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Updated: Feb 4, 2026

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
Published on: January 6, 2015
Bacterial dynamin-like proteins reveal mechanism for membrane fusion
1Ludwig-Maximilians-Universität München, Fakultät Biologie, Großhaderner Straße 2-4, 82152, Planegg-Martinsried, Germany. marc.bramkamp@lmu.de.
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.
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