Team:HokkaidoU Japan/Aggregation
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Team:HokkaidoU Japan
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When you harvest E. coli on your laboratory, is there a efficiently way to aggregate E. coli with the SAP? We would like to try to suggest a possibility of the expression of E. coli aggregation by expression of the SAP fused to 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 flagella. So we think that the aggregation of E. coli because of the bindings between the flagella 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.
If the method for industrial production of self-assembling peptides by using E. coli is established, it will contribute to disperse the utilization of hydrogel. To achieve this, we should focus on the synthesis and transportation of self-assembling peptides. We mentioned about “Transportation” above. Furthermore, we hope that other teams make further developments regarding “Synthesis”.And also the aggregation methods for E. coli in lab may be improved in the aspects of the cost or efficiency. From this aspects, the simpler methods without utilizing Ag43, His- tag, or RADA16-I are desirable. We expect that the understanding about the differences of the aggregating efficiency among the methods utilizing these proteins will be expanded. In addition, we hope that the aggregation method for E. coli by utilizing the self-assembling peptides we proposed will be useful in the future.
[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 a efficiently way to aggregate E. coli with the SAP? We would like to try to suggest a possibility of the expression of E. coli aggregation by expression of the SAP fused to 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
E. coli are aggregated by the binding through SAP. SAP is expressed on the fllagerum. |
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 flagella. So we think that the aggregation of E. coli because of the bindings between the flagella 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 filament of E. coli
Any protein can be inserted into the FliC. |
If the method for industrial production of self-assembling peptides by using E. coli is established, it will contribute to disperse the utilization of hydrogel. To achieve this, we should focus on the synthesis and transportation of self-assembling peptides. We mentioned about “Transportation” above. Furthermore, we hope that other teams make further developments regarding “Synthesis”.And also the aggregation methods for E. coli in lab may be improved in the aspects of the cost or efficiency. From this aspects, the simpler methods without utilizing Ag43, His- tag, or RADA16-I are desirable. We expect that the understanding about the differences of the aggregating efficiency among the methods utilizing these proteins will be expanded. In addition, we hope that the aggregation method for E. coli by utilizing the self-assembling peptides we proposed will be useful in the future.
[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.
