Document Detail

Bacterial beta-lactamase fragmentation complementation strategy can be used as a method for identifying interacting protein pairs.
MedLine Citation:
PMID:  18156775     Owner:  NLM     Status:  MEDLINE    
We investigated the applicability of the TEM-1 beta- lactamase fragment complementation (BFC) system to develop a strategy for the screening of protein-protein interactions in bacteria. A BFC system containing a human Fas-associated death domain (hFADD) and human Fas death domain (hFasDD) was generated. The hFADD-hFasDD interaction was verified by cell survivability in ampicillin-containing medium and the colorimetric change of nitrocefin. It was also confirmed by His pull-down assay using cell lysates obtained in selection steps. A coiled-coil helix coiled-coil domain-containing protein 5 (CHCH5) was identified as an interacting protein of human uracil DNA glycosylase (hUNG) from the bacterial BFC cDNA library strategy. The interaction between hUNG and CHCH5 was further confirmed with immunoprecipitation using a mammalian expression system. CHCH5 enhanced the DNA glycosylase activity of hUNG to remove uracil from DNA duplexes containing a U/G mismatch pair. These results suggest that the bacterial BFC cDNA library strategy can be effectively used to identify interacting protein pairs.
Jong-Hwa Park; Jung Ho Back; Soo Hyun Hahm; Hye-Young Shim; Min Ju Park; Sung Il Ko; Ye Sun Han
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of microbiology and biotechnology     Volume:  17     ISSN:  1017-7825     ISO Abbreviation:  J. Microbiol. Biotechnol.     Publication Date:  2007 Oct 
Date Detail:
Created Date:  2007-12-24     Completed Date:  2008-02-28     Revised Date:  2008-08-22    
Medline Journal Info:
Nlm Unique ID:  9431852     Medline TA:  J Microbiol Biotechnol     Country:  Korea (South)    
Other Details:
Languages:  eng     Pagination:  1607-15     Citation Subset:  IM    
Department of Advanced Technology Fusion and Bio/Molecular Informatics Center, Konkuk University, Seoul, Korea.
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MeSH Terms
Amino Acid Sequence
Base Sequence
Cell Line
Chromatography, Affinity
Escherichia coli / genetics
Fas-Associated Death Domain Protein / metabolism
Gene Library
Genetic Complementation Test / methods*
Molecular Sequence Data
Protein Binding
Protein Interaction Domains and Motifs
Recombinant Fusion Proteins / genetics,  metabolism
Sensitivity and Specificity
Sequence Alignment
Two-Hybrid System Techniques
Uracil-DNA Glycosidase / chemistry,  genetics,  metabolism
beta-Lactamases / genetics*,  metabolism*
Reg. No./Substance:
0/Fas-Associated Death Domain Protein; 0/Recombinant Fusion Proteins; EC 3.2.2.-/Uracil-DNA Glycosidase; EC; EC TEM-1

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