Part:BBa_K2082105

Cytidin deaminase 1 from Pteromyzon marinus

Biology

Cytidin deaminases (cda) are DNA editing enzymes in eukaryotes, which have multiple functions like the generation of antibody diversity, defence against retroviruses and demethylation during development (Lada et al. 2011). The main activity of CDAs is the deamination from cytidin to uracil in CG base pairs. The resulting UG base pairs split in replication in one CG and one UA basepair (Figure 1). Therefore, the main mutations created by CDAs are C → T transitions.
Figure 1: 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

K2082105 was used in our genome wide mutator BBa_K2082117. It s effect was increased by coexpression of the uracil glycosylase inhibitor BBa_K2082104.

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References

• Lada, A. G.; Krick, C. Frahm; Kozmin, S. G.; Mayorov, V. I.; Karpova, T. S.; Rogozin, I. B.; Pavlov, Y. I. (2011): Mutator effects and mutation signatures of editing deaminases produced in bacteria and yeast. In Biochemistry. Biokhimiia 76 (1), pp. 131–146.

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
  INCOMPATIBLE WITH RFC[1000]

  Illegal BsaI site found at 283