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!align=left |Citation | |||
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'''Shiomi, D and Margolin, W''' (2007) The C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli.''J. Bacteriol.'' '''189''':236-43 | |||
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!align=left |Abstract | |||
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In Escherichia coli, the Min system, consisting of three proteins, MinC, MinD, and MinE, negatively regulates FtsZ assembly at the cell poles, helping to ensure that the Z ring will assemble only at midcell. Of the three Min proteins, MinC is sufficient to inhibit Z-ring assembly. By binding to MinD, which is mostly localized at the membrane near the cell poles, MinC is sequestered away from the cell midpoint, increasing the probability of Z-ring assembly there. Previously, it has been shown that the two halves of MinC have two distinct functions. The N-terminal half is sufficient for inhibition of FtsZ assembly, whereas the C-terminal half of the protein is required for binding to MinD as well as to a component of the division septum. In this study, we discovered that overproduction of the C-terminal half of MinC (MinC(122-231)) could also inhibit cell division and that this inhibition was at the level of Z-ring disassembly and dependent on MinD. We also found that fusing green fluorescent protein to either the N-terminal end of MinC(122-231), the C terminus of full-length MinC, or the C terminus of MinC(122-231) perturbed MinC function, which may explain why cell division inhibition by MinC(122-231) was not detected previously. These results suggest that the C-terminal half of MinC has an additional function in the regulation of Z-ring assembly. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17085577 PubMed] | |||
Online version:[http://dx.doi.org/10.1128/JB.00666-06 10.1128/JB.00666-06] | |||
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!align=left |Keywords | |||
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Adenosine Triphosphatases; Cell Division; Escherichia coli; Escherichia coli Proteins; Membrane Proteins; Protein Structure, Tertiary | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | |||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
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==See also== | |||
==References== | |||
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Revision as of 21:27, 20 May 2012
| Citation |
Shiomi, D and Margolin, W (2007) The C-terminal domain of MinC inhibits assembly of the Z ring in Escherichia coli.J. Bacteriol. 189:236-43 |
|---|---|
| Abstract |
In Escherichia coli, the Min system, consisting of three proteins, MinC, MinD, and MinE, negatively regulates FtsZ assembly at the cell poles, helping to ensure that the Z ring will assemble only at midcell. Of the three Min proteins, MinC is sufficient to inhibit Z-ring assembly. By binding to MinD, which is mostly localized at the membrane near the cell poles, MinC is sequestered away from the cell midpoint, increasing the probability of Z-ring assembly there. Previously, it has been shown that the two halves of MinC have two distinct functions. The N-terminal half is sufficient for inhibition of FtsZ assembly, whereas the C-terminal half of the protein is required for binding to MinD as well as to a component of the division septum. In this study, we discovered that overproduction of the C-terminal half of MinC (MinC(122-231)) could also inhibit cell division and that this inhibition was at the level of Z-ring disassembly and dependent on MinD. We also found that fusing green fluorescent protein to either the N-terminal end of MinC(122-231), the C terminus of full-length MinC, or the C terminus of MinC(122-231) perturbed MinC function, which may explain why cell division inhibition by MinC(122-231) was not detected previously. These results suggest that the C-terminal half of MinC has an additional function in the regulation of Z-ring assembly. |
| Links |
PubMed Online version:10.1128/JB.00666-06 |
| Keywords |
Adenosine Triphosphatases; Cell Division; Escherichia coli; Escherichia coli Proteins; Membrane Proteins; Protein Structure, Tertiary |
| edit table |
Significance
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Useful Materials and Methods
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