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Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast
Published on: February 20, 2017
Different patterns of integral membrane protein localization during cell division in Bacillus subtilis
D H Meredith1, M Plank1, P J Lewis1
1School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW 2308, Australia.
Microbiology (Reading, England)
|January 5, 2008
Summary
Bacterial cell division involves assembling many proteins at the cell mid-point. This study shows that while most membrane proteins can still move, some, like ATP synthase, are excluded from the division site.
Area of Science:
- Microbiology
- Cell Biology
- Biochemistry
Background:
- Bacterial cell division is a complex process, precisely regulated at the cell's mid-point.
- Formation of the FtsZ ring and associated proteins is crucial for cytokinesis.
- Integral membrane proteins typically diffuse freely but may be affected during division.
Purpose of the Study:
- To investigate the localization and diffusion of integral membrane proteins in Bacillus subtilis during cell division.
- To determine if the assembly of division proteins excludes other membrane proteins from the mid-cell region.
Main Methods:
- Localization studies of integral membrane proteins in Bacillus subtilis.
- Analysis of protein distribution at the mid-cell during the onset of division.
Main Results:
- The recruitment of division and septum-specific proteins does not universally prevent the diffusion of other integral membrane proteins.
- Specific proteins, including ATP synthase and succinate dehydrogenase, were found to be reduced or absent at the mid-cell during division.
- This exclusion may be linked to associations with phosphatidylglycerol-rich lipid domains, which are less abundant at division sites.
Conclusions:
- Bacterial cell division site assembly does not completely halt membrane protein diffusion.
- Certain proteins are selectively excluded from the division site, potentially due to lipid domain interactions.
- This selective exclusion may play a role in regulating membrane composition during bacterial cytokinesis.
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