Team:HSNU-TAIPEI/Composite Part

Composite Part

AFB1

  • BBa_K1613000J22106+B0032
  • BBa_K1613001J23119+B0032
  • BBa_K1613002J22106+B0034
  • BBa_K1613003CYP1A2+B0015

    ↑gel electrophoresis BBa_K1613003

  • BBa_K1613005J23119+B0030+CYP1A2+B0015

    ↑gel electrophoresis BBa_K1613005

  • BBa_K1613006J23119+B0032+CYP1A2+B0015

    • √ A composite part that can detect some toxins.

    cyp1a2 can oxidize the substances that it can metabolism. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. CYP1A2 is able to metabolize some PAHs to carcinogenic intermediates. Other xenobiotic substrates for this enzyme include aflatoxin B1, and acetaminophen.

  • BBa_K1613007J23119+B0034+CYP1A2+B0015

    • √ A composite part that can detect some toxins.

    cyp1a2 can oxidize the substances that it can metabolism. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. CYP1A2 is able to metabolize some PAHs to carcinogenic intermediates. Other xenobiotic substrates for this enzyme include aflatoxin B1, and acetaminophen.

  • BBa_K1613008J22106+B0032+E0040+B0015
  • BBa_K1613009J22106+B0032+E1010+B0015
  • BBa_K1613010J22106+B0034+E0040+B0015
  • BBa_K1613011J22106+B0034+E1010+B0015

Benzo[a]pyrene

  • BBa_K1613012J23113+B0034+K1092104+B0034+K1092000+B0015

    • √ QsrR Binding Site inhibits the transcription and translation of Red Fluorescent Protein.

    There is a QsrR Binding Site between promoter and RBS. Which can combine with Quinone-sensing and response Repressor(QsrR). And inhibit the transcription. While QsrR combines with BaP-1,6-Quinone, the QsrR will be activated and depart the Binding Site. That makes the transcription of downstream.

  • BBa_K1613013J23113+B0034+E1010+B0015

    ↑gel electrophoresis BBa_K1613012+BBa_K1613013

Cadmium

  • BBa_K1613014K896008+B0032+E1010+B0015
  • BBa_K1613015K896008+B0032+E0040+B0015
  • BBa_K1613016K896008+B0032

    • √ is a new part which can detect cadmium in ions in the liquid.

    This part is designed to proceed cadmium detection in e.coli.Zintp K896008 is a promoter which is designed by NYMU in 2013.It is a part highly specific to the cadmium.The promoter can trigger the RFP. We combine these part to detect cadmium.

Lead

  • BBa_K1613017

    • √ K1613017 is a new part which can detect lead (Pb) ions in the liquid.

    This part is desinged to proceed lead detection in e.coli. When lead ions (Pb2+) enter the e.coli, they will combine with the protein PbrR and then form a dimer. The lead promoter can be controlled by the dimer to further trigger the RFP. The idea of this design came from Brown 2007 igem team, also working on lead detection. We combined I721001 and I721002 from their teams with a constitutive promoter J23102 and RFP to make them function.

  • BBa_S05295B0015+I721001

    ↑gel electrophoresis BBa_S05295

  • BBa_S05296B0032+I721002

    ↑gel electrophoresis BBa_S05296

Copper

  • BBa_K1613018K1555000+B0030+E1010+B0015

    • √ Device with CopA promoter to detect copper

    This is a device to detect copper. We use the CopA Promoter to detect (Promoter from BBa_K1555000) because it’s more specific and sensitive than MarO, CueO. We linked it with RBS, RFP, and Terminator.

Mercury

  • BBa_K1613019J23102+B0034+K1420002+K1420004+K346002+B0032+E1010+B0015

    • √ It can detect methyl mercury.

    MerB can turn Methyl mercury into Hg2+.MerR can combine with Hg2+ and change the structure of DNA. And DNA can be trancripted easier. PmerT is controlled by MerR. PmerT cannot be transcripted because MerR changes the shape of PmerT. In short, the whole reaction will continue if MerR combines with Hg2+.

  • BBa_K1613021J23102+B0034+K1420002+K1420004
  • BBa_K1613022K346002+B0032+E1010+B0015

    • √ BBa_K1613020,a composite part which has PmerT,B0032,RFP and B0015.

    PmerT is controlled by MerR. PmerT cannot be transcripted because MerR changes the shape of PmerT. In short, the whole reaction will continue if MerR combines with Hg2+.