Coding

Part:BBa_K2082104

Designed by: Carsten Hain   Group: iGEM16_Bielefeld-CeBiTec   (2016-10-14)


Uracil glycosylase inhibitor


Biology

The uracil glycosylase inhibitor (ugi) inhibits the uracil glycosylase (UNG) by mimicing the structure of UNGs natural substrate, abasic DNA sites (Figure 1). This results in inhibition of UNG and thereby the UNG initiated base excision repair (Figure 2). Consequently ugi overexpression leads to a mutator phenotype by imparing a DNA fidelity mechanism.
Figure 1: Structural alignment of ugi (red) and DNA with an abasic site (blue). The structural alignment between ugi and DNA with an abasic site show the structural mimicry of ugi, which leads to the inhibition of uracil DNA glycosylase (green).

Figure 2: Deamination of cytidin by cytidin deasminases and possible resulting mutations by replication of base excision repair (BER). Cytidin deaminase (CDA) deaminases cytidin to uracil. The resulting GU base pair leads to a UA and a CG base pair during replication. Alternatively, the uracil is repaired via the base excision repair. Thereby, uracil-DNA-glycosylase (UNG) cuts out uracil and the abasic site (AP-site) inside the DNA gets repaired by specialized endonucleases and polymerases.

Application

K2082104 was used in our genome wide mutator BBa_K2082117, increasing the mutating capabilities of the cytidin deaminase BBa_K2082105.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


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Categories
Parameters
None