ArticleACS synthetic biology2019
A Multireporter Bacterial 2-Hybrid Assay for the High-Throughput and Dynamic Assay of PDZ Domain-Peptide Interactions.
Article in ACS synthetic biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Mint/X11 PDZ domains from non-bilaterian animals recognize and bind CaScientific reports · 2024Article
- Molecular determinants of TRAF6 binding specificity suggest that native interaction partners are not optimized for affinity.Protein science : a publication of the Protein Society · 2022Article
- Luminescence complementation assay for measurement of binding to protein C-termini in live cells.Analytical biochemistry · 2020Article
- The geometric influence on the Cys2His2 zinc finger domain and functional plasticity.Nucleic acids research · 2020Article
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8 authors.
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Abstract
The accurate determination of protein-protein interactions has been an important focus of molecular biology toward which much progress has been made due to the continuous development of existing and new technologies. However, current methods can have limitations, including scale and restriction to high affinity interactions, limiting our understanding of a large subset of these interactions. Here, we describe a modified bacterial-hybrid assay that employs combined selectable and scalable reporters that enable the sensitive screening of large peptide libraries followed by the sorting of positive interactions by the level of reporter output. We have applied this tool to characterize a set of human and E. coli PDZ domains. Our results are consistent with prior characterization of these proteins, and the improved sensitivity increases our ability to predict known and novel in vivo binding partners. This approach allows for the recovery of a wide range of affinities with a high throughput method that does not sacrifice the scale of the screen.
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