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A bacterial dynamin-like protein mediating nucleotide-independent membrane fusion.
Mol Microbiol. 2011 Mar; 79(5):1294-304
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26 Jan 2011
Cecile Sauvanet
F1000 Cell Biology
Weill Institute for Cell and Molecular Biology - Cornell University,
Ithaca, USA.
F1000 Cell Biology
Weill Institute for Cell and Molecular Biology - Cornell University,
Ithaca, USA.
DOI: 10.3410/f.7945956.8306054
We found this article interesting because it points to a potential role for bacterial dynamins in membrane fusion events.
This work shows that the protein DynA of Bacillus subtilis is a dynamin-like GTPase, the hydrolytic activity of which requires its two subunits D1 and D2 (each carrying a GTPase domain)...Continue reading
This work shows that the protein DynA of Bacillus subtilis is a dynamin-like GTPase, the hydrolytic activity of which requires its two subunits D1 and D2 (each carrying a GTPase domain)...Continue reading
We found this article interesting because it points to a potential role for bacterial dynamins in membrane fusion events.
This work shows that the protein DynA of Bacillus subtilis is a dynamin-like GTPase, the hydrolytic activity of which requires its two subunits D1 and D2 (each carrying a GTPase domain), which can be further stimulated through self-assembly. DynA can bind, dock and merge membranes independently of GTP. In addition, DynA-mediated membrane fusion depends only on the presence of magnesium ions in the solution and, surprisingly, membrane fusion events are reduced two-fold in the presence of GTP. Membrane binding, docking and merging events seem to rely solely on the D1 subunit of the DynA molecule. Further work is needed to elucidate the exact role of the D1 and D2 subunits of DynA in membrane remodeling events (e.g. through systematic electron microscopy [EM] studies on liposomes in the presence of these fragments), as well as the role of magnesium ions on the structure of DynA and/or apposing membranes.
This work shows that the protein DynA of Bacillus subtilis is a dynamin-like GTPase, the hydrolytic activity of which requires its two subunits D1 and D2 (each carrying a GTPase domain), which can be further stimulated through self-assembly. DynA can bind, dock and merge membranes independently of GTP. In addition, DynA-mediated membrane fusion depends only on the presence of magnesium ions in the solution and, surprisingly, membrane fusion events are reduced two-fold in the presence of GTP. Membrane binding, docking and merging events seem to rely solely on the D1 subunit of the DynA molecule. Further work is needed to elucidate the exact role of the D1 and D2 subunits of DynA in membrane remodeling events (e.g. through systematic electron microscopy [EM] studies on liposomes in the presence of these fragments), as well as the role of magnesium ions on the structure of DynA and/or apposing membranes.
Disclosures
None declared
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Tareste D and Sauvanet C: F1000Prime Recommendation of [Bürmann F et al., Mol Microbiol 2011, 79(5):1294-304]. In F1000Prime, 26 Jan 2011; DOI: 10.3410/f.7945956.8306054. F1000Prime.com/7945956#eval8306054
F1000Prime Recommendations, Dissents and Comments for [Bürmann F et al., Mol Microbiol 2011, 79(5):1294-304]. In F1000Prime, 25 May 2013; F1000Prime.com/7945956
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Dynamins are a family of large GTPases that are involved in key cellular processes, where they mediate events of membrane fission and fusion. The dynamin superfamily is not restricted to eukaryotes but might have a bacterial origin, with many species containing an operon of two genes related to mitofusins. However, it is not clear whether bacterial dynamins promote membrane fission or fusion. The dynamin-like protein DynA of Bacillus subtilis is remarkable in that it arose from a gene fusion of two dynamins and contains two separate dynamin-like subunits and GTPase domains. We found that DynA exhibits strictly auto-regulated GTP hydrolysis, and that progress through the GTPase cycle is concerted within DynA oligomers. Furthermore, we show that DynA can tether membranes and mediates nucleotide-independent membrane fusion in vitro. This process merely requires magnesium as a cofactor. Our results provide a set of minimal requirements for membrane fusion by dynamin-like proteins and have mechanistic implications in particular for the fusion of mitochondria.
© 2011 Blackwell Publishing Ltd.
DOI: 10.1111/j.1365-2958.2011.07523.x
PMID: 21205012
