NDRG2's interaktion med Api5: NDRG2's Interaction with Api5

Freya Armstrong, Annaleigh Ohrt Fehler, Cecilie Felicia Hansen, Louise Justesen, Katrine Aagaard Myhr, Mathias Mørup-Lendal & Sebastian Niemeier

Studenteropgave: Semesterprojekt

Abstrakt

Background: Studies show that the tumor suppressor gene N-myc downstream regulated gene 2 (NDRG2) is downregulated in cancer cells, whereas the anti-apoptosis gene Apoptosis Inhibitor 5 (Api5) is upregulated. Furthermore it is established that there is a complex formation between NDRG2 and Api5. The complex formation might result in a blockage of Api5´s function as an inhibitor of E2 promoter binding factor (E2F) induced apoptosis. Therefore one may suggest that NDRG2 indirectly induces apoptosis and thereby counteracts uncontrolled cell proliferation. Hypothesis: The Api5 binding site in NDRG2 is to be found in one of the following regions, the α-helix 6 domain or after the α/β-hydrolase domain. Methods: Based on the hypothesis two mutations are incorporated in the regions mentioned above in which it is possible to examine whether the interaction between NDRG2 and Api5 is still possible. To examine whether complex formation occurs, a yeast-2-hybrid assay is used. Initial experiments are necessary to incorporate the mutations in plasmids which are used in the yeast-2-hybrid assay. Results: Incorporation of mutations and conduction of plasmids was successful. When the α-helix 6 domain was mutated, no complex formation between NDRG2 and Api5 occurred. The complex formation was not affected by the mutation after the α/β-hydrolase domain. Conclusion: The results indicate that the α-helix 6 domain in NDRG2 is essential for the binding to Api5.

UddannelserBasis - Naturvidenskabelig Bacheloruddannelse, (Bachelor uddannelse) Basis
SprogDansk
Udgivelsesdato19 jun. 2012

Emneord

  • Api5
  • Gær-2-hybridsystem
  • E2F
  • NDRG2