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Cell Physiol Biochem. 2007;20(6):703-14.

New fast BiFC plasmid assay system for in vivo protein-protein interactions.

Author information

1
Department of Biochemistry and Molecular Biology, BK21 Project for Medical Science, Institute of Genetic Science, Yonsei University School of Medicine, Seoul (Korea).

Abstract

In this age of massive genetic and protein information, a fast and reliable method of studying in vivo protein-protein interactions is necessary. We have developed a novel system that can overcome limitations of existing assay methods. This new method adopts two existing systems for fast analysis of diverse protein-protein interactions. For rapid, large-scale cloning, we adopted the Gateway system and developed novel destination vectors containing YFP N-terminus (YN) or YFP C-terminus (YC) to visualize protein-protein interactions in vivo using bimolecular fluorescence complementation (BiFC). Using this system, we investigated molecular interactions among the three POZ-domain regulatory proteins mAPM-1, LRF, KLHL10 that belong to a subgroup of human POZ-domain proteins, and showed that the POZ-domains of mAPM-1, LRF and KLHL10 could form both homodimers and heterodimers. This new method is a highly efficient, sensitive and specific assay method for protein-protein interaction in vivo.

PMID:
17982253
DOI:
10.1159/000110431
[Indexed for MEDLINE]
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