Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 13, Pages 11236-11241Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.194365
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Funding
- European Commission [HEALTH-F3-2009-223431]
- Ministerio de Ciencia e Innovacion Plan Nacional (Spain) [BIO2008-04478-C03-00]
- Comunidad de Madrid COMBACT [S-BIO-0260/2006]
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We have incorporated, for the first time, FtsZ and FtsA (the soluble proto-ring proteins from Escherichia coli) into bacterial giant unilamellar inner membrane vesicles (GUIMVs). Inside the vesicles, the structural organization and spatial distribution of fluorescently labeled FtsZ and FtsA were determined by confocal microscopy. We found that, in the presence of GDP, FtsZ was homogeneously distributed in the lumen of the vesicle. In the presence of GTP analogs, FtsZ assembled inside the GUIMVs, forming a web of dense spots and fibers. Whereas isolated FtsA was found adsorbed to the inner face of GUIMVs, the addition of FtsZ together with GTP analogs resulted in its dislodgement and its association with the FtsZ fibers in the lumen, suggesting that the FtsA-membrane interaction can be modulated by FtsZ polymers. The use of this novel in vitro system to probe interactions between divisome components will help to determine the biological implications of these findings.
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