Team:Warsaw/Stage2/Background

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<h2>MinC</h2>
<h2>MinC</h2>
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<div class="note">Sed purus neque, suscipit vitae, cursus vitae, porttitor non, dui. Mauris volutpat dui vitae sapien. Duis laoreet nibh vitae sem.</div>
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<div class="note">Natural role:</div>
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<p>Natural role:
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<p>
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MinC is the component of MinCDE system. Together with nucleoid occlusion it ensures that cell division will occur in the middle of a cell. Three proteins – MinC, MinD and MinE play different role[s] in preventing formation of division complex too close to cell poles [1]. MinC is directly responsible for stopping the early stage of division by inhibiting the polymerysation [polymerization] of FtsZ protein monomers into [a] structure known as [the] Z-ring [8].   
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MinC is the component of MinCDE system. Together with nucleoid occlusion it ensures that cell division will occur in the middle of a cell. Three proteins – MinC, MinD and MinE play different roles in preventing formation of division complex too close to cell poles [1]. MinC is directly responsible for stopping the early stage of division by inhibiting the polymerization of FtsZ protein monomers into a structure known as the Z-ring [8].</p>  
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FtsZ is [a] tubuline homologue capable of creating chains, lariats and rings independent[ly] from [of] other cellular factors [3]. The stability and decay of these structures is dependent on GTPase activity of  FtsZ proteins [7]. In [at] the beginning of cell division FtsZ monomers form the Z-ring to which other proteins responsible for the division are recruited. The presence of N-terminal domain of MinC prevents establishing additional Z-rings [9] [additional Z-rings from forming/being established].
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<p>FtsZ is a tubuline homologue capable of creating chains, lariats and rings independently of other cellular factors [3]. The stability and decay of these structures is dependent on GTPase activity of  FtsZ proteins [7]. At the beginning of cell division FtsZ monomers form the Z-ring to which other proteins responsible for the division are recruited. The presence of N-terminal domain of MinC prevents additional Z-rings from being established [9].</p>
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In bacterial cells MinC is recruited to membrane by the second protein of the system – MinD. This process involves C-terminal domain of MinC, which is also responsible for oligomerisation of MinC [its oligomerisation]. Recrutation [recruitment] to membrane is necessary for the inhibiting effect to occur at the physiological concentration of protein [4]. Finally the third protein – MinE [-] is responsible for keeping the MinCD complex from acting in the midcell region[,] thus enabling the formation of Z-ring in the proper location [5].   
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<center><img src="https://static.igem.org/mediawiki/2010/8/89/F3_sm.jpg"></center>
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It was shown that mutants in either minC or minD divide at cell pole much more often than wild type, resulting in creation of nucleoid-free minicells. This mutations, however are not lethal because enough of the cells in population divide properly to sustain growth [6].
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<i><p> MinCDE system and nucleoid occlusion[10]. </p></i>
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<p> In bacterial cells MinC is recruited to membrane by the second protein of the system – MinD. This process involves C-terminal domain of MinC, which is also responsible for its oligomerisation. Recruitment to membrane is necessary for the inhibiting effect to occur at the physiological concentration of protein [4]. Finally the third protein - MinE - is responsible for keeping the MinCD complex from acting in the midcell region, thus enabling the formation of Z-ring in the proper location [5].   
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It was shown that mutants in either <i>minC</i> or <i>minD</i> divide at cell pole much more often than wild type, resulting in creation of nucleoid-free minicells. This mutations, however are not lethal because enough of the cells in population divide properly to sustain growth [6].</p>
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Natural occurrence:
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<div class="note">Natural occurrence:</div>
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Although MinCDE is mostly analysed in E.coli, it’s elements were found in many different bacteria groups including Proteobacteria, Deinococcus-Thermus and Firmicutes phyla [1]. In B. subtilis the MinE protein is replaced by DivIVa which locates itself at the cell poles and with help of MinJ binds MinCD complex, decreasing it’s concentration at midcell [2].
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<p> Although MinCDE is mostly analysed in <i>E.coli</i>, it’s elements were found in many different bacteria groups including <i>Proteobacteria</i>, <i>Deinococcus-Thermus</i> and <i>Firmicutes</i> <i>phyla</i> [1]. In <i>B. subtilis</i> the MinE protein is replaced by DivIVa which locates itself at the cell poles and with help of MinJ binds MinCD complex, decreasing it’s concentration at midcell [2]. </p>
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Application in synthetic biology:
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<div class="note">Application in synthetic biology:</div>
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<p>
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When expressed at high level MinC is capable of preventing bacterial cell from dividing. As a result, of this the cell becomes filamentus. This effect requires only high level of MinC, not MinD. It has been proven that overexpression of C-terminal domain of MinC alone is sufficient to inhibit cell division [9]. Recent findings suggest also, that MinC originated from <i>E.coli</i> is able to function properly in <i>B.subtilis</i> and inhibit its division [11].</p>
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When expressed at high level MinC is capable of preventing bacteria[l] cell from dividing. As a result, of this [the] cell become[s] filamentus. These [this] effect requires only high level of MinC, not MinD. It was [has been] proven that overexpression of C-terminal domain of MinC alone is sufficient to inhibit cell division [9].
 
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<div class="note">References:</div>
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References:
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<p>1. “Themes and variations in prokaryotic cell division”, William Margolin, FEMS Microbiology Reviews 24 (2000) 531-548  </p>
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<p>2. “The MinCDJ System in Bacillus subtilis Prevents Minicell Formation by Promoting Divisome Disassembly”, Suey van Baarle and Marc Bramkami, PLoS One. 5 (2010)</p>
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1. “Themes and variations in prokaryotic cell division”, William Margolin, FEMS Microbiology Reviews 24 (2000) 531-548   
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<p>3. “The bacterial cell division protein FtsZ assembles into cytoplasmic ring in fission yeast”, Ramanujam Srinivasan et al. Genes Dev. 22 (2008) 1741-1746</p>
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2. “The MinCDJ System in Bacillus subtilis Prevents Minicell Formation by Promoting Divisome Disassembly”, Suey van Baarle and Marc Bramkami, PLoS One. 5 (2010)
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<p>4. “The Switch I and II Regions of MinD Are Required for Binding and Activating MinC”, Huaijin Zhou and Joe Lutkenhaus, J Bacteriol. 186 (2004) 1546–1555.</p>
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3. “The bacterial cell division protein FtsZ assembles into cytoplasmic ring in fission yeast”, Ramanujam Srinivasan et al. Genes Dev. 22 (2008) 1741-1746
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<p>5. “The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle.”, Fu X et al. Proc. Natl. Acad. Sci. U S A 98. (2001)</p>
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4. “The Switch I and II Regions of MinD Are Required for Binding and Activating MinC”, Huaijin Zhou and Joe Lutkenhaus, J Bacteriol. 186 (2004) 1546–1555.
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<p>6. “FtsZ ring cluster in min and partition mutants: Role of both the Min system and the nucleoid in regulation FtsZ ring location”, Yu et al. Mol. Microbiol. 32 (1999) 315-326</p>
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5. “The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle.”, Fu X et al. Proc. Natl. Acad. Sci. U S A 98. (2001)  
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<p>7. “FtsZ from Divergent Foreign Bacteria Can Function for Cell Division in Escherichia coli”, Masaki Osawa and Harold P. Erickson, J. Bacteriol. 188 (2006) 7132-7140</p>
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6. “FtsZ ring cluster in min and partition mutants: Role of both the Min system and the nucleoid in regulation FtsZ ring location”, Yu et al. Mol. Microbiol. 32 (1999) 315-326
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<p>8. “FtsZ, a tubulin homologue in prokaryote division”, Harold P. Erickson.Trends. Cell Biol. 7 (1997) 362-367</p>
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7. “FtsZ from Divergent Foreign Bacteria Can Function for Cell Division in Escherichia coli”, Masaki Osawa and Harold P. Erickson, J. Bacteriol. 188 (2006) 7132-7140
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<p>9. “Analysis of MinC Reveals Two Independent Domains Involved in Interaction with MinD and FtsZ”, Zonglin Hu and Joe Lutkenhaus, J. Bacteriol. 182 (2000) 3965-3971</p>
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8. “FtsZ, a tubulin homologue in prokaryote division”, Trends. Cell Biol. 7 (1997) 362-367
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<p>10. "Synchronization of Chromosome Dynamics and Cell Division in Bacteria", Martin Thanbichler, doi: 10.1101/cshperspect.a000331(2009) </p>
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9. “Analysis of MinC Reveals Two Independent Domains Involved in Interaction with MinD and FtsZ”, J. Bacteriol. 182 (2000) 3965-3971</p>
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<p>11. "Expression of Escherichia coli Min system in Bacillus subtilis and its effect on cell division" Nad'a Pavlendová, Katarína Muchová, Imrich Barák FEMS Microbiology Letters, 302 (2010) 58-68</p>
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Latest revision as of 15:16, 27 October 2010

Example Tabs

MinC

Natural role:

MinC is the component of MinCDE system. Together with nucleoid occlusion it ensures that cell division will occur in the middle of a cell. Three proteins – MinC, MinD and MinE play different roles in preventing formation of division complex too close to cell poles [1]. MinC is directly responsible for stopping the early stage of division by inhibiting the polymerization of FtsZ protein monomers into a structure known as the Z-ring [8].

FtsZ is a tubuline homologue capable of creating chains, lariats and rings independently of other cellular factors [3]. The stability and decay of these structures is dependent on GTPase activity of FtsZ proteins [7]. At the beginning of cell division FtsZ monomers form the Z-ring to which other proteins responsible for the division are recruited. The presence of N-terminal domain of MinC prevents additional Z-rings from being established [9].

MinCDE system and nucleoid occlusion[10].

In bacterial cells MinC is recruited to membrane by the second protein of the system – MinD. This process involves C-terminal domain of MinC, which is also responsible for its oligomerisation. Recruitment to membrane is necessary for the inhibiting effect to occur at the physiological concentration of protein [4]. Finally the third protein - MinE - is responsible for keeping the MinCD complex from acting in the midcell region, thus enabling the formation of Z-ring in the proper location [5]. It was shown that mutants in either minC or minD divide at cell pole much more often than wild type, resulting in creation of nucleoid-free minicells. This mutations, however are not lethal because enough of the cells in population divide properly to sustain growth [6].

Natural occurrence:

Although MinCDE is mostly analysed in E.coli, it’s elements were found in many different bacteria groups including Proteobacteria, Deinococcus-Thermus and Firmicutes phyla [1]. In B. subtilis the MinE protein is replaced by DivIVa which locates itself at the cell poles and with help of MinJ binds MinCD complex, decreasing it’s concentration at midcell [2].

Application in synthetic biology:

When expressed at high level MinC is capable of preventing bacterial cell from dividing. As a result, of this the cell becomes filamentus. This effect requires only high level of MinC, not MinD. It has been proven that overexpression of C-terminal domain of MinC alone is sufficient to inhibit cell division [9]. Recent findings suggest also, that MinC originated from E.coli is able to function properly in B.subtilis and inhibit its division [11].

References:

1. “Themes and variations in prokaryotic cell division”, William Margolin, FEMS Microbiology Reviews 24 (2000) 531-548

2. “The MinCDJ System in Bacillus subtilis Prevents Minicell Formation by Promoting Divisome Disassembly”, Suey van Baarle and Marc Bramkami, PLoS One. 5 (2010)

3. “The bacterial cell division protein FtsZ assembles into cytoplasmic ring in fission yeast”, Ramanujam Srinivasan et al. Genes Dev. 22 (2008) 1741-1746

4. “The Switch I and II Regions of MinD Are Required for Binding and Activating MinC”, Huaijin Zhou and Joe Lutkenhaus, J Bacteriol. 186 (2004) 1546–1555.

5. “The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle.”, Fu X et al. Proc. Natl. Acad. Sci. U S A 98. (2001)

6. “FtsZ ring cluster in min and partition mutants: Role of both the Min system and the nucleoid in regulation FtsZ ring location”, Yu et al. Mol. Microbiol. 32 (1999) 315-326

7. “FtsZ from Divergent Foreign Bacteria Can Function for Cell Division in Escherichia coli”, Masaki Osawa and Harold P. Erickson, J. Bacteriol. 188 (2006) 7132-7140

8. “FtsZ, a tubulin homologue in prokaryote division”, Harold P. Erickson.Trends. Cell Biol. 7 (1997) 362-367

9. “Analysis of MinC Reveals Two Independent Domains Involved in Interaction with MinD and FtsZ”, Zonglin Hu and Joe Lutkenhaus, J. Bacteriol. 182 (2000) 3965-3971

10. "Synchronization of Chromosome Dynamics and Cell Division in Bacteria", Martin Thanbichler, doi: 10.1101/cshperspect.a000331(2009)

11. "Expression of Escherichia coli Min system in Bacillus subtilis and its effect on cell division" Nad'a Pavlendová, Katarína Muchová, Imrich Barák FEMS Microbiology Letters, 302 (2010) 58-68

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