Abstract
To screen the protein interacting with apoptin from human leucocyte cDNA library by using yeast two-hybrid system, four clones interacting with apoptin were identified. One of them was homologous with Nmi (N-Myc interaction protein). Cell co-immunoprecipitation showed that apoptin could bind to Nmi in mammalian cells. Apoptin mutants T1, T2 and T3 lacked the C-terminal 11 AA, 33-46 AA and both, respectively. Apoptin mutants T2 and T3 failed to interact with Nmi, suggesting that its 33-46 AA was pivotal for the interaction. Apoptin mutant T1 still interacted with Nmi, suggesting that its C-terminal 11 AA was not essential for the interaction.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 369-372 |
| Number of pages | 4 |
| Journal | Acta biochimica et biophysica Sinica |
| Volume | 34 |
| Issue number | 3 |
| State | Published - 2002 |
Keywords
- Apoptin
- Co-immunoprecipitation
- Nmi
- Yeast two-hybrid
ASJC Scopus subject areas
- Biophysics
- Biochemistry
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Sun, G. J., Tong, X., Dong, Y., Mei, Z. Z., & Sun, Z. X. (2002). Identification of a protein interacting with apoptin from human leucocyte cDNA library by using yeast two-hybrid screening. Acta biochimica et biophysica Sinica, 34(3), 369-372.