Difference between revisions of "Part:BBa K4619001:Design"
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The original pobA/R operon consists of six main components: pobA, pobA RBS, pobA/R dual-directional promoter, pobR operator, pobR RBS, and pobR. The pobA gene encodes an unnecessary enzyme that breaks down 4-HBA. Therefore, we remove the pobA and pobA RBS components but retain the entire promoter, pobR RBS, and pobR. | The original pobA/R operon consists of six main components: pobA, pobA RBS, pobA/R dual-directional promoter, pobR operator, pobR RBS, and pobR. The pobA gene encodes an unnecessary enzyme that breaks down 4-HBA. Therefore, we remove the pobA and pobA RBS components but retain the entire promoter, pobR RBS, and pobR. |
Revision as of 15:29, 9 October 2023
PobR
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 462
Illegal AgeI site found at 154
Illegal AgeI site found at 675 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 595
Design Notes
<https://static.igem.wiki/teams/4619/wiki/wetlab/finewu/pobr-description1.png,width=90%;>
The original pobA/R operon consists of six main components: pobA, pobA RBS, pobA/R dual-directional promoter, pobR operator, pobR RBS, and pobR. The pobA gene encodes an unnecessary enzyme that breaks down 4-HBA. Therefore, we remove the pobA and pobA RBS components but retain the entire promoter, pobR RBS, and pobR.
Regarding the original digitizer, we eliminate the XylS system, which includes the XylS protein and its corresponding promoter. We then combine these two sections and anticipate that the new chimeric digitizer will function properly.
We use GFP to test our new chimeric digitizer. If it functions well, we will replace GFP with luxI to establish our bio-sensor.
Source
DiMarco, A. A., Averhoff, B., & Ornston, L. N. (1993). Identification of the transcriptional activator pobR and characterization of its role in the expression of pobA, the structural gene for p-hydroxybenzoate hydroxylase in Acinetobacter calcoaceticus. 175(14), 4499-4506. doi:doi:10.1128/jb.175.14.4499-4506.1993