Difference between revisions of "Team:HokkaidoU Japan/Aggregation"
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| − | <br> When you harvest <span style="font-style: italic">E.coli</span> on your laboratory, is there the way to aggregate <span style="font-style: italic">E.coli</span> efficiently with the SAP? We try to suggest the expression of the SAP on <span style="font-style: italic">E. coli</span> flagellum. Perhaps, a new method for the <span style="font-style: italic">E.coli</span> aggregation, except for Ag43 which has been adopted by some iGEM teams[1][2], may be found. | + | <br> When you harvest <span style="font-style: italic">E. coli</span> on your laboratory, is there the way to aggregate <span style="font-style: italic">E. coli</span> efficiently with the SAP? We try to suggest the expression of the SAP on <span style="font-style: italic">E. coli</span> flagellum. Perhaps, a new method for the <span style="font-style: italic">E. coli</span> aggregation, except for Ag43 which has been adopted by some iGEM teams[1][2], may be found. |
</span> | </span> | ||
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<td style="border-style: none"; align="center"><h2>Fig. 1. Image of aggregation using SAP | <td style="border-style: none"; align="center"><h2>Fig. 1. Image of aggregation using SAP | ||
| − | <br><span style="font-style: italic">E.coli</span> are aggregated by the binding through SAP. SAP is expressed on the fllagerum.</h2></td> | + | <br><span style="font-style: italic">E. coli</span> are aggregated by the binding through SAP. SAP is expressed on the fllagerum.</h2></td> |
</tr> | </tr> | ||
</table> | </table> | ||
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| − | <br>FliC is an important domain which forms the filament (Fig. 2)[3]. It is known that any protein can be inserted into its domain without losing the function of the flagellar. So we think that the aggregation of <span style="font-style: italic">E.coli</span> because of the bindings between the flagellar is likely to happen by inserting SAP, for example, RADA16-I and P<span class="sitatuki">11</span>-4. Since it has been reported that the overexpression of the Ag43 decreases the survival rate of E.coli, we have to search for an alternative method for the aggregation of <span style="font-style: italic">E.coli</span>. | + | <br>FliC is an important domain which forms the filament (Fig. 2)[3]. It is known that any protein can be inserted into its domain without losing the function of the flagellar. So we think that the aggregation of <span style="font-style: italic">E. coli</span> because of the bindings between the flagellar is likely to happen by inserting SAP, for example, RADA16-I and P<span class="sitatuki">11</span>-4. Since it has been reported that the overexpression of the Ag43 decreases the survival rate of E. coli, we have to search for an alternative method for the aggregation of <span style="font-style: italic">E. coli</span>. |
| − | <br>Therefore we propose that inserting the SAP has an advantage of improving the efficiency of the consecutive chemical reactions when <span style="font-style: italic">E.coli</span> which have different functions approach each other. | + | <br>Therefore we propose that inserting the SAP has an advantage of improving the efficiency of the consecutive chemical reactions when <span style="font-style: italic">E. coli</span> which have different functions approach each other. |
</span> | </span> | ||
<br> | <br> | ||
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</tr> | </tr> | ||
<tr> | <tr> | ||
| − | <td style="border-style: none"; align="center"><h2>Fig. 2. Image of <span style="font-style: italic">E.coli</span>'s | + | <td style="border-style: none"; align="center"><h2>Fig. 2. Image of <span style="font-style: italic">E. coli</span>'s filament |
<br>Any protein can be inserted into the FliC.</h2></td> | <br>Any protein can be inserted into the FliC.</h2></td> | ||
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| − | <br> There may still be room for improvement for the financial aspect or the efficiency regarding the way to harvest <span style="font-style: italic">E.coli</span> in the laboratory. And a more simple method would be much more desirable without any expensive biological device. At last we wish that | + | <br> There may still be room for improvement for the financial aspect or the efficiency regarding the way to harvest <span style="font-style: italic">E. coli</span> in the laboratory. And a more simple method would be much more desirable without any expensive biological device. At last we wish that more research will be conducted of the difference between the efficiency of the aggregation of <span style="font-style: italic">E. coli</span> with the biological tools, for example Ag43, RADA16-I, and P<span class="sitatuki">11</span>-4. And we also desire for the possibility of the aggregation of <span style="font-style: italic">E. coli</span> with the SAP we suggest. |
</span> | </span> | ||
Revision as of 12:35, 19 October 2016
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Team:HokkaidoU Japan
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When you harvest E. coli on your laboratory, is there the way to aggregate E. coli efficiently with the SAP? We try to suggest the expression of the SAP on E. coli flagellum. Perhaps, a new method for the E. coli aggregation, except for Ag43 which has been adopted by some iGEM teams[1][2], may be found.
FliC is an important domain which forms the filament (Fig. 2)[3]. It is known that any protein can be inserted into its domain without losing the function of the flagellar. So we think that the aggregation of E. coli because of the bindings between the flagellar is likely to happen by inserting SAP, for example, RADA16-I and P11-4. Since it has been reported that the overexpression of the Ag43 decreases the survival rate of E. coli, we have to search for an alternative method for the aggregation of E. coli.
Therefore we propose that inserting the SAP has an advantage of improving the efficiency of the consecutive chemical reactions when E. coli which have different functions approach each other.
There may still be room for improvement for the financial aspect or the efficiency regarding the way to harvest E. coli in the laboratory. And a more simple method would be much more desirable without any expensive biological device. At last we wish that more research will be conducted of the difference between the efficiency of the aggregation of E. coli with the biological tools, for example Ag43, RADA16-I, and P11-4. And we also desire for the possibility of the aggregation of E. coli with the SAP we suggest.
[1] HokkaidoU Japan 2012
[2] Aberdeen Scotland 2014
[3] Kuwajima, G. 1988. Construction of a minimum-size functional flagellin of Escherichia coli. J. Bacteriol. 170:3305–3309.
When you harvest E. coli on your laboratory, is there the way to aggregate E. coli efficiently with the SAP? We try to suggest the expression of the SAP on E. coli flagellum. Perhaps, a new method for the E. coli aggregation, except for Ag43 which has been adopted by some iGEM teams[1][2], may be found.
 |
Fig. 1. Image of aggregation using SAP
|
FliC is an important domain which forms the filament (Fig. 2)[3]. It is known that any protein can be inserted into its domain without losing the function of the flagellar. So we think that the aggregation of E. coli because of the bindings between the flagellar is likely to happen by inserting SAP, for example, RADA16-I and P11-4. Since it has been reported that the overexpression of the Ag43 decreases the survival rate of E. coli, we have to search for an alternative method for the aggregation of E. coli.
Therefore we propose that inserting the SAP has an advantage of improving the efficiency of the consecutive chemical reactions when E. coli which have different functions approach each other.
 |
Fig. 2. Image of E. coli's filament
|
There may still be room for improvement for the financial aspect or the efficiency regarding the way to harvest E. coli in the laboratory. And a more simple method would be much more desirable without any expensive biological device. At last we wish that more research will be conducted of the difference between the efficiency of the aggregation of E. coli with the biological tools, for example Ag43, RADA16-I, and P11-4. And we also desire for the possibility of the aggregation of E. coli with the SAP we suggest.
[1] HokkaidoU Japan 2012
[2] Aberdeen Scotland 2014
[3] Kuwajima, G. 1988. Construction of a minimum-size functional flagellin of Escherichia coli. J. Bacteriol. 170:3305–3309.
