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A Split-Luciferase Reporter Recognizing GFP and mCherry Tags to Facilitate Studies of Protein–Protein Interactions

Title: A Split-Luciferase Reporter Recognizing GFP and mCherry Tags to Facilitate Studies of Protein–Protein Interactions
Authors: Mehdi Moustaqil; Akshay Bhumkar; Laura Gonzalez; Lisa Raoul; Dominic J. B. Hunter; Pascal Carrive; Emma Sierecki; Yann Gambin
Source: International Journal of Molecular Sciences, Vol 18, Iss 12, p 2681 (2017)
Publisher Information: MDPI AG
Publication Year: 2017
Collection: Directory of Open Access Journals: DOAJ Articles
Subject Terms: protein–protein interaction; split-luciferase; universal reporter; Leishmania tarentolae cell-free; Biology (General); QH301-705.5; Chemistry; QD1-999
Description: The use of fluorescently-tagged proteins in microscopy has become routine, and anti-GFP (Green fluorescent protein) affinity matrices are increasingly used in proteomics protocols. However, some protein–protein interactions assays, such as protein complementation assays (PCA), require recloning of each protein as a fusion with the different parts of the complementation system. Here we describe a generic system where the complementation is separated from the proteins and can be directly used with fluorescently-tagged proteins. By using nanobodies and performing tests in cell-free expression systems, we accelerated the development of multiple reporters, detecting heterodimers and homodimers or oligomers tagged with GFP or mCherry. We demonstrate that the system can detect interactions at a broad range of concentrations, from low nanomolar up to micromolar.
Document Type: article in journal/newspaper
Language: English
Relation: https://www.mdpi.com/1422-0067/18/12/2681; https://doaj.org/toc/1422-0067; https://doaj.org/article/67cea85b4efd4bf38d7b3901b180e724
DOI: 10.3390/ijms18122681
Availability: https://doi.org/10.3390/ijms18122681; https://doaj.org/article/67cea85b4efd4bf38d7b3901b180e724
Accession Number: edsbas.B2CCE08F
Database: BASE