Screening of protein interacting with apoptin by yeast two-hybrid from human leucocyte cDNA library

Guo Jing Sun, Xin Tong, Xiang Bing Meng, Yan Dong, Zhi Xian Sun*

*Corresponding author for this work

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Using yeast two-hybrid system to screen the protein interacting with apoptin from human leucocyte cDNA library, four clones interacting with apoptin were identified. One of them was homologue with ABP280 (actin-binding protein), ABP280 is a dimeric actin crossing protein and plays a key role in stabilizing the membrane-cytoskeleton. Cell co-immunoprecipitation showed that apoptin could bind to ABP280 in mammalian cells. Apoptin mutants T1, T2 and T3 lack the C-terminal 11 amino acid, 33-46 amino acid and both respectively. Apoptin mutants T2 and T3 failed to interact with ABP280, which revealed that its 33-46 amino acid was pivotal for the interaction. Apoptin mutant T1 still interacted with ABP280, which revealed that its C-terminal 11 amino acid was not essential for the interaction.

Original languageEnglish (US)
Number of pages1
JournalProgress in Biochemistry and Biophysics
Volume28
Issue number5
StatePublished - Dec 1 2001

Keywords

  • ABP280
  • Apoptin
  • Yeast two-hybridization
  • co-immunoprecipitation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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