Team:Warsaw/Stage2/Background

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<h2>Safety</h2>
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<h2>MinC</h2>
<div class="note">Sed purus neque, suscipit vitae, cursus vitae, porttitor non, dui. Mauris volutpat dui vitae sapien. Duis laoreet nibh vitae sem.</div>
<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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<p>Suspendisse magna dui, porta in, condimentum at, molestie nec, augue. Quisque vulputate facilisis ipsum.  Aenean sollicitudin quam sed ante. Donec at nunc. In hac habitasse platea dictumst. Suspendisse quis lorem sit amet eros congue volutpat. Nam laoreet ultricies pede. Nulla vestibulum, pede eget varius vestibulum, nisl mi aliquet nisl, eget eleifend quam dui faucibus tortor. Maecenas justo. In lacus nisl, tempus at, aliquam nec, ornare in, metus. Maecenas hendrerit mauris vitae purus. Cras id sem.</p>
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<p>Natural role:
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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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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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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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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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Natural occurrence:
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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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Application in synthetic biology:
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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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References:
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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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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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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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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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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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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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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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8. “FtsZ, a tubulin homologue in prokaryote division”, Trends. Cell Biol. 7 (1997) 362-367
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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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Revision as of 14:26, 22 October 2010

Example Tabs

MinC

Sed purus neque, suscipit vitae, cursus vitae, porttitor non, dui. Mauris volutpat dui vitae sapien. Duis laoreet nibh vitae sem.

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 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]. 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]. 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]. 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 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]. 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”, Trends. Cell Biol. 7 (1997) 362-367 9. “Analysis of MinC Reveals Two Independent Domains Involved in Interaction with MinD and FtsZ”, J. Bacteriol. 182 (2000) 3965-3971

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