ArticleProtein science : a publication of the Protein Society2007
A bacterial two-hybrid system based on the twin-arginine transporter pathway of E. coli.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 44 citations in OpenAlex.
- Peptide Aptamer PA3 Attenuates the Viability ofFrontiers in microbiology · 2022Article
- Selection of Protein-Protein Interactions of Desired Affinities with a Bandpass Circuit.Journal of molecular biology · 2019Article
- An engineered genetic selection for ternary protein complexes inspired by a natural three-component hitchhiker mechanism.Scientific reports · 2014Article
- Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Microbiology and molecular biology reviews : MMBR · 2012Review
- A transferable heterogeneous two-hybrid system in Escherichia coli based on polyhydroxyalkanoates synthesis regulatory protein PhaR.Microbial cell factories · 2011Article
- Versatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome.FEMS microbiology reviews · 2009Review
- Exploration of twin-arginine translocation for expression and purification of correctly folded proteins in Escherichia coli.Microbial biotechnology · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We have developed a bacterial two-hybrid system for the detection of interacting proteins that capitalizes on the folding quality control mechanism of the Twin Arginine Transporter (Tat) pathway. The Tat export pathway is responsible for the membrane translocation of folded proteins, including proteins consisting of more than one polypeptide, only one of which contains a signal peptide ("hitchhiker export"). Here, one protein (bait) is expressed as a fusion to a Tat signal peptide, whereas the second protein (prey) is fused to a protein reporter that can confer a phenotype only after export into the bacterial periplasmic space. Since the prey-reporter fusion lacks a signal peptide, it can only be exported as a complex with the bait-signal peptide fusion that is capable of targeting the Tat translocon. Using maltose-binding protein as a reporter, clones expressing interacting proteins can be grown on maltose minimal media or on MacConkey plates. In addition, we introduce the use of the cysteine disulfide oxidase DsbA as a reporter. Export of a signal peptide-prey:bait-DsbA complex into the periplasm allows complementation of dsbA(-) mutants and restores the formation of active alkaline phosphatase, which in turn can be detected by a chromogenic assay.
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