Identification of a protein interacting with apoptin from human leucocyte cDNA library by using yeast two-hybrid screening

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...

Full description

Saved in:
Bibliographic Details
Published inSheng wu hua hsüeh yü sheng wu wu li hsüeh pao Vol. 34; no. 3; p. 369
Main Authors Sun, G J, Tong, X, Dong, Y, Mei, Z Z, Sun, Z X
Format Journal Article
LanguageChinese
Published China 01.05.2002
Subjects
Capsid - genetics
Capsid - metabolism
Capsid Proteins
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Gene Library
Humans
Intracellular Signaling Peptides and Proteins
Leukocytes - metabolism
Mutation
Precipitin Tests
Saccharomyces cerevisiae
Two-Hybrid System Techniques
Online AccessGet more information

Cover

More Information
Summary: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.
ISSN:0582-9879