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

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Dynamin-like proteins (DLPs) form flexible tetramers that bridge bacterial membranes. This tetramerization activates GTPase activity, enabling membrane tethering and tube formation, revealing a mechanism for membrane remodeling.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Dynamin-like proteins (DLPs) are GTPases crucial for membrane restructuring.
  • Heterotypic oligomerization of DLPs, like mitofusins, is known to bridge and fuse membranes.
  • Bacterial DLP gene pairing suggests a role for heterotypic oligomerization in membrane remodeling.

Purpose of the Study:

  • To elucidate the structural mechanism of bacterial DLP heterotypic pairs in membrane tethering.
  • To investigate the functional consequences of DLP heterotypic complex formation.

Main Methods:

  • X-ray crystallography to determine the structure of a Campylobacter jejuni DLP heterotypic pair.
  • In vitro biochemical assays to assess GTPase activity and lipid binding.
  • Liposome-based experiments to observe membrane tethering and tubulation.

Main Results:

  • The crystal structure revealed a 2:2 stoichiometric tetramer formed by back-to-back assembly of heterodimers.
  • This tetrameric structure exhibits significant flexibility due to a random coil linker.
  • Tetramerization triggered GTPase activity and lipid binding, leading to liposome tethering and tube formation in vitro.

Conclusions:

  • A direct mechanism for long-range membrane binding and bridging by bacterial DLP pairs is proposed.
  • The flexible tetrameric structure is key to the observed membrane remodeling functions.
  • Findings offer broad mechanistic and structural insights applicable to other heterotypic DLP complexes.