Literature DB >> 11842428

Identifying and modifying protein-DNA and protein-protein interactions using a bacterial two-hybrid selection system.

J K Joung1.   

Abstract

A bacterial two-hybrid system based on transcriptional activation in E. coli has recently been described. A variety of different protein-DNA and protein-protein interactions from bacteria, yeast, and humans have been studied using this bacterial-based system. The method, because it is based in bacteria, offers significant advantages relative to its yeast counterpart including the ability to analyze complex libraries > 10(8) in size, ease of use, and speed. The ability to easily and rapidly process very large libraries make this system a powerful tool for identifying, modifying, or optimizing protein-DNA and protein-protein interactions. Copyright 2002 Wiley-Liss, Inc.

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Year:  2001        PMID: 11842428     DOI: 10.1002/jcb.10065

Source DB:  PubMed          Journal:  J Cell Biochem Suppl        ISSN: 0733-1959


  3 in total

Review 1.  Chlamydomonas reinhardtii at the crossroads of genomics.

Authors:  Arthur R Grossman; Elizabeth E Harris; Charles Hauser; Paul A Lefebvre; Diego Martinez; Dan Rokhsar; Jeff Shrager; Carolyn D Silflow; David Stern; Olivier Vallon; Zhaoduo Zhang
Journal:  Eukaryot Cell       Date:  2003-12

2.  The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like B.

Authors:  Bing Wang; Jerry Pelletier; Michel J Massaad; Annette Herscovics; Gordon C Shore
Journal:  Mol Cell Biol       Date:  2004-04       Impact factor: 4.272

3.  Synthetic protein-protein interaction domains created by shuffling Cys2His2 zinc-fingers.

Authors:  Astrid V Giesecke; Rui Fang; J Keith Joung
Journal:  Mol Syst Biol       Date:  2006-03-21       Impact factor: 11.429

  3 in total

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